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56 hits found for Kim

SASDCJ2 – Solution structure of recombinant prion protein (89–230) in complex with Fab-P

Major prion proteinP-Clone Fab, Chimera experimental SAS data
PDB model
Sample: Major prion protein monomer, 23 kDa Mus musculus protein
P-Clone Fab, Chimera monomer, 47 kDa Homo sapiens protein
Buffer: sodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl), pH: 5.1
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2013 Dec 5
Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Biophys J 109(4):793-805 (2015)
...Kim SJ, Schneidman-Duhovny D, Stöhr J, Poncet-Montange G, Weiss TM, Tsuruta H, Prusiner SB, Sali A
RgGuinier 3.9 nm
Dmax 14.5 nm
VolumePorod 106 nm3

SASDDQ2 – EspG3 chaperone from Mycobacterium marinum

EspG3 chaperone from Mycobacterium marinum M experimental SAS data
EspG3 chaperone from Mycobacterium marinum M Kratky plot
Sample: EspG3 chaperone from Mycobacterium marinum M monomer, 32 kDa Mycobacterium marinum M protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
...Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.3 nm
Dmax 8.0 nm

SASDDR2 – EspG1 chaperone from Mycobacterium marinum

EspG1 from Mycobacterium marinum experimental SAS data
EspG1 from Mycobacterium marinum Kratky plot
Sample: EspG1 from Mycobacterium marinum monomer, 30 kDa Mycobacterium marinum protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
...Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.7 nm
Dmax 9.7 nm

SASDDS2 – EspG3 chaperone from Mycobacter smegmatis

EspG3 chaperone from Mycobacterium smegmatis experimental SAS data
EspG3 chaperone from Mycobacterium smegmatis Kratky plot
Sample: EspG3 chaperone from Mycobacterium smegmatis monomer, 32 kDa Mycobacterium smegmatis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
...Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.5 nm
Dmax 8.6 nm

SASDDT2 – EspG3 chaperone from Mycobacterium tuberculosis

EspG3 chaperone from Mycobacterium tuberculosis experimental SAS data
EspG3 chaperone from Mycobacterium tuberculosis Kratky plot
Sample: EspG3 chaperone from Mycobacterium tuberculosis , 34 kDa Mycobacterium tuberculosis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
...Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.5 nm
Dmax 9.0 nm

SASDDU2 – EspG3 chaperone from Mycobacterium smegmatis (Sel-Met labelled)

EspG3 chaperone from Mycobacterium smegmatis experimental SAS data
EspG3 chaperone from Mycobacterium smegmatis Kratky plot
Sample: EspG3 chaperone from Mycobacterium smegmatis monomer, 32 kDa Mycobacterium smegmatis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
...Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.6 nm
Dmax 9.2 nm

SASDDV2 – EspG5 chaperone from Mycobacterium tuberculosis

EspG5 chaperone from Mycobacterium tuberculosis experimental SAS data
EspG5 chaperone from Mycobacterium tuberculosis Rg histogram
Sample: EspG5 chaperone from Mycobacterium tuberculosis monomer, 32 kDa Mycobacterium tuberculosis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jan 12
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
...Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.4 nm
Dmax 8.0 nm

SASDDW2 – EspG5-PE25/PPE41 complex from M. tuberculosis

EspG5 chaperone from Mycobacterium tuberculosisPE25 from Mycobacterium tuberculosisPPE41 from Mycobacterium tuberculosis experimental SAS data
Sample: EspG5 chaperone from Mycobacterium tuberculosis monomer, 32 kDa Mycobacterium tuberculosis protein
PE25 from Mycobacterium tuberculosis monomer, 11 kDa Mycobacterium tuberculosis protein
PPE41 from Mycobacterium tuberculosis monomer, 22 kDa Mycobacterium tuberculosis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Feb 10
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
...Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 4.0 nm
Dmax 13.0 nm

SASDDX2 – EspG3-PE5/PPE4 complex from M. tuberculosis

EspG3 chaperone from Mycobacterium tuberculosisPE5 from Mycobacterium tuberculosisPPE4 from Mycobacterium tuberculosis experimental SAS data
Sample: EspG3 chaperone from Mycobacterium tuberculosis , 34 kDa Mycobacterium tuberculosis protein
PE5 from Mycobacterium tuberculosis monomer, 10 kDa Mycobacterium tuberculosis protein
PPE4 from Mycobacterium tuberculosis monomer, 52 kDa Mycobacterium tuberculosis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2015 Jun 15
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
...Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 4.0 nm
Dmax 14.2 nm

SASDF53 – Bruton's Tyrosine Kinase - kinase domain

Bruton's tyrosine kinase, kinase domain experimental SAS data
DAMMIN model
Sample: Bruton's tyrosine kinase, kinase domain monomer, 32 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms Nature Communications 11(1) (2020)
...Kim H, Dal Peraro M, Hantschel O
RgGuinier 2.1 nm
Dmax 6.8 nm
VolumePorod 52 nm3

SASDF63 – Bruton's Tyrosine Kinase - SH2-kinase domain

Bruton's tyrosine kinase - Src homolgy domain 2 - kinase domain experimental SAS data
Bruton's Tyrosine Kinase - SH2-kinase domain Rg histogram
Sample: Bruton's tyrosine kinase - Src homolgy domain 2 - kinase domain monomer, 46 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Nov 3
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms Nature Communications 11(1) (2020)
...Kim H, Dal Peraro M, Hantschel O
RgGuinier 2.8 nm
Dmax 9.4 nm
VolumePorod 64 nm3

SASDF73 – Bruton's Tyrosine Kinase - SH3-SH2-kinase domain

Bruton's tyrosine kinase - Src homology 3-2 kinase domain experimental SAS data
Bruton's Tyrosine Kinase - SH3-SH2-kinase domain Rg histogram
Sample: Bruton's tyrosine kinase - Src homology 3-2 kinase domain monomer, 52 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Nov 2
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms Nature Communications 11(1) (2020)
...Kim H, Dal Peraro M, Hantschel O
RgGuinier 2.6 nm
Dmax 8.3 nm
VolumePorod 72 nm3

SASDF83 – Bruton's Tyrosine Kinase - Full-length

Bruton's tyrosine kinase - full length experimental SAS data
Bruton's Tyrosine Kinase - Full-length Rg histogram
Sample: Bruton's tyrosine kinase - full length monomer, 77 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Nov 3
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms Nature Communications 11(1) (2020)
...Kim H, Dal Peraro M, Hantschel O
RgGuinier 4.0 nm
Dmax 15.6 nm
VolumePorod 114 nm3

SASDH93 – Braveheart Fragment 1

Braveheart Fragment 1 experimental SAS data
DAMMIN model
Sample: Braveheart Fragment 1 monomer, 116 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 8.4 nm
Dmax 24.0 nm
VolumePorod 426 nm3

SASDHA3 – Braveheart Fragment 2

Braveheart Fragment 2 experimental SAS data
DAMMIN model
Sample: Braveheart Fragment 2 monomer, 112 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 8.1 nm
Dmax 27.2 nm
VolumePorod 443 nm3

SASDHB3 – Braveheart Fragment 3

Braveheart Fragment 3 experimental SAS data
DAMMIN model
Sample: Braveheart Fragment 3 monomer, 111 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 6.5 nm
Dmax 20.5 nm
VolumePorod 492 nm3

SASDHC3 – Braveheart in 0 mM MgCl2

Braveheart RNA experimental SAS data
DAMMIN model
Sample: Braveheart RNA monomer, 205 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 9.9 nm
Dmax 30.0 nm
VolumePorod 2150 nm3

SASDHD3 – Braveheart in 6 mM MgCl2

Braveheart RNA experimental SAS data
DAMMIN model
Sample: Braveheart RNA monomer, 205 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Dec 16
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 11.8 nm
Dmax 28.7 nm
VolumePorod 2380 nm3

SASDHE3 – Braveheart in 12 mM MgCl2

Braveheart RNA experimental SAS data
DAMMIN model
Sample: Braveheart RNA monomer, 205 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 12 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jul 20
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 9.7 nm
Dmax 26.0 nm
VolumePorod 1370 nm3

SASDEF3 – Paenibacillus xanthan lyase (PXL) at 4 °C

Paenibacillus xanthan lyase experimental SAS data
Paenibacillus xanthan lyase Kratky plot
Sample: Paenibacillus xanthan lyase monomer, 113 kDa Paenibacillus sp-62047 protein
Buffer: 20 mM Tris,, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 15
Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. Cell Chem Biol 26(2):191-202.e6 (2019)
Jensen PF, Kadziola A, Comamala G, Segura DR, Anderson L, Poulsen JN, Rasmussen KK, Agarwal S, Sainathan RK, Monrad RN, Svendsen A, Nielsen JE, Lo Leggio L, Rand KD
RgGuinier 3.7 nm
Dmax 13.1 nm
VolumePorod 137 nm3

SASDHF3 – Braveheart 5' module in 6 mM MgCl2

Braveheart 5' Module experimental SAS data
DAMMIN model
Sample: Braveheart 5' Module monomer, 32 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Dec 16
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 4.3 nm
Dmax 13.5 nm
VolumePorod 71 nm3

SASDEG3 – Paenibacillus xanthan lyase (PXL) at 20 °C

Paenibacillus xanthan lyase experimental SAS data
Paenibacillus xanthan lyase Kratky plot
Sample: Paenibacillus xanthan lyase monomer, 113 kDa Paenibacillus sp-62047 protein
Buffer: 20 mM Tris,, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 15
Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. Cell Chem Biol 26(2):191-202.e6 (2019)
Jensen PF, Kadziola A, Comamala G, Segura DR, Anderson L, Poulsen JN, Rasmussen KK, Agarwal S, Sainathan RK, Monrad RN, Svendsen A, Nielsen JE, Lo Leggio L, Rand KD
RgGuinier 3.8 nm
Dmax 13.8 nm
VolumePorod 134 nm3

SASDHG3 – Braveheart 5' module in 12 mM MgCl2

Braveheart 5' Module experimental SAS data
DAMMIN model
Sample: Braveheart 5' Module monomer, 32 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 12 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Dec 16
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 4.8 nm
Dmax 15.0 nm
VolumePorod 99 nm3

SASDHH3 – Braveheart 3' module in 6 mM MgCl2

Braveheart 3' module experimental SAS data
DAMMIN model
Sample: Braveheart 3' module monomer, 72 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Dec 16
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 6.5 nm
Dmax 18.5 nm
VolumePorod 198 nm3

SASDHJ3 – Braveheart 3' module in 12 mM MgCl2

Braveheart 3' module experimental SAS data
DAMMIN model
Sample: Braveheart 3' module monomer, 72 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 12 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Dec 16
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 7.3 nm
Dmax 19.0 nm
VolumePorod 219 nm3

SASDHK3 – Braveheart RNA + Cellular nucleic acid-binding protein (CNBP)

Braveheart RNACellular nucleic acid-binding protein experimental SAS data
DAMMIN model
Sample: Braveheart RNA monomer, 205 kDa Homo sapiens RNA
Cellular nucleic acid-binding protein monomer, 22 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 9.8 nm
Dmax 30.2 nm
VolumePorod 1660 nm3

SASDHL3 – Braveheart Fragment 1 + Cellular nucleic acid-binding protein (CNBP)

Cellular nucleic acid-binding proteinBraveheart Fragment 1 experimental SAS data
DAMMIN model
Sample: Cellular nucleic acid-binding protein monomer, 22 kDa Homo sapiens protein
Braveheart Fragment 1 monomer, 116 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 8.2 nm
Dmax 27.0 nm
VolumePorod 455 nm3

SASDH44 – 3' Complex of XPA-DBD and RPA70AB

DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit3-prime  Nucleotide Excision Repair Junction Model Substrate experimental SAS data
HADDOCK model
Sample: DNA repair protein complementing XP-A cells monomer, 17 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 27 kDa Homo sapiens protein
3-prime Nucleotide Excision Repair Junction Model Substrate monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 17 Nov 2
A key interaction with RPA orients XPA in NER complexes. Nucleic Acids Res (2020)
...Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ
RgGuinier 3.1 nm
Dmax 9.7 nm
VolumePorod 103 nm3

SASDH54 – 5' Complex of XPA-DBD with RPA70AB

DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit5-prime Nucleotide Excision Repair Junction Model Substrate experimental SAS data
HADDOCK model
Sample: DNA repair protein complementing XP-A cells monomer, 17 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 27 kDa Homo sapiens protein
5-prime Nucleotide Excision Repair Junction Model Substrate monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 4
A key interaction with RPA orients XPA in NER complexes. Nucleic Acids Res (2020)
...Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ
RgGuinier 2.9 nm
Dmax 97.0 nm
VolumePorod 87 nm3

SASDHL4 – N-terminal domains 1-5 of the cation-independent mannose-6-phosphate receptor (CI-MPR)

Cation-independent mannose-6-phosphate receptor experimental SAS data
Cation-independent mannose-6-phosphate receptor Kratky plot
Sample: Cation-independent mannose-6-phosphate receptor monomer, 81 kDa Homo sapiens protein
Buffer: 20 mM imidazole, 150 mM NaCl, 5 mM beta glycerol phosphate, 10 mM MnCl2, pH: 6.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Oct 12
Allosteric regulation of lysosomal enzyme recognition by the cation-independent mannose 6-phosphate receptor (2020)
...Kim J, Tiemeyer M, Ren G, Sharp J, Dahms N
RgGuinier 3.7 nm
Dmax 10.1 nm
VolumePorod 140 nm3

SASDHM4 – N-terminal domains 1-5 of the cation-independent mannose-6-phosphate receptor (CI-MPR) from SEC-SAXS

Cation-independent mannose-6-phosphate receptor experimental SAS data
Cation-independent mannose-6-phosphate receptor Kratky plot
Sample: Cation-independent mannose-6-phosphate receptor monomer, 81 kDa Homo sapiens protein
Buffer: 20 mM imidazole, 150 mM NaCl, 5 mM beta glycerol phosphate, 10 mM MnCl2, pH: 6.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Nov 12
Allosteric regulation of lysosomal enzyme recognition by the cation-independent mannose 6-phosphate receptor (2020)
...Kim J, Tiemeyer M, Ren G, Sharp J, Dahms N
RgGuinier 3.7 nm
Dmax 13.5 nm
VolumePorod 147 nm3

SASDHN4 – N-terminal 5 domains of the cation-independent mannose-6-phosphate receptor (CI-MPR) bound to mannose 6-phosphate (M6P)

Cation-independent mannose-6-phosphate receptor experimental SAS data
Cation-independent mannose-6-phosphate receptor Kratky plot
Sample: Cation-independent mannose-6-phosphate receptor monomer, 81 kDa Homo sapiens protein
Buffer: 20 mM imidazole, 150 mM NaCl, 5 mM beta glycerol phosphate, 10 mM MnCl2, pH: 6.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Nov 12
Allosteric regulation of lysosomal enzyme recognition by the cation-independent mannose 6-phosphate receptor (2020)
...Kim J, Tiemeyer M, Ren G, Sharp J, Dahms N
RgGuinier 3.7 nm
Dmax 13.3 nm
VolumePorod 150 nm3

SASDHP4 – Palmitoyl-protein thioesterase 1 (PPT1)

Palmitoyl-protein thioesterase 1 experimental SAS data
Palmitoyl-protein thioesterase 1 Kratky plot
Sample: Palmitoyl-protein thioesterase 1 monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM imidazole, 150 mM NaCl, 5 mM beta glycerol phosphate, 10 mM MnCl2, pH: 6.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Nov 12
Allosteric regulation of lysosomal enzyme recognition by the cation-independent mannose 6-phosphate receptor (2020)
...Kim J, Tiemeyer M, Ren G, Sharp J, Dahms N
RgGuinier 2.3 nm
Dmax 9.8 nm
VolumePorod 54 nm3

SASDHQ4 – N-terminal domains 1-5 of the cation-independent mannose-6-phosphate receptor (CI-MPR) in complex with palmitoyl-protein thioesterase 1 (PPT1)

Cation-independent mannose-6-phosphate receptorPalmitoyl-protein thioesterase 1 experimental SAS data
Cation-independent mannose-6-phosphate receptor Palmitoyl-protein thioesterase 1 Kratky plot
Sample: Cation-independent mannose-6-phosphate receptor monomer, 81 kDa Homo sapiens protein
Palmitoyl-protein thioesterase 1 monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM imidazole, 150 mM NaCl, 5 mM beta glycerol phosphate, 10 mM MnCl2, pH: 6.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Nov 12
Allosteric regulation of lysosomal enzyme recognition by the cation-independent mannose 6-phosphate receptor (2020)
...Kim J, Tiemeyer M, Ren G, Sharp J, Dahms N
RgGuinier 4.9 nm
Dmax 19.3 nm
VolumePorod 258 nm3

SASDCM6 – Small GTPase Rab5 conjugated with ubiquitin at K116

Monoubiquitinated Rab5 at K165 experimental SAS data
Small GTPase Rab5 conjugated with ubiquitin at K116 Rg histogram
Sample: Monoubiquitinated Rab5 at K165 monomer, 32 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 10 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2016 Nov 21
Site-specific monoubiquitination downregulates Rab5 by disrupting effector binding and guanine nucleotide conversion. Elife 6 (2017)
...Kim G, Baek J, Park SH, Choi CY, Lee S
RgGuinier 2.6 nm
Dmax 8.7 nm

SASDCN6 – Small GTPase Rab5 conjugated with ubiquitin at K140

Monoubiquitinated Rab5 at K165 experimental SAS data
Small GTPase Rab5 conjugated with ubiquitin at K140 Rg histogram
Sample: Monoubiquitinated Rab5 at K165 monomer, 32 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 10 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2016 Nov 21
Site-specific monoubiquitination downregulates Rab5 by disrupting effector binding and guanine nucleotide conversion. Elife 6 (2017)
...Kim G, Baek J, Park SH, Choi CY, Lee S
RgGuinier 2.3 nm
Dmax 8.4 nm

SASDCP6 – Small GTPase Rab5 conjugated with ubiquitin at K165

Monoubiquitinated Rab5 at K165 experimental SAS data
Small GTPase Rab5 conjugated with ubiquitin at K165 Rg histogram
Sample: Monoubiquitinated Rab5 at K165 monomer, 32 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 10 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2016 Nov 21
Site-specific monoubiquitination downregulates Rab5 by disrupting effector binding and guanine nucleotide conversion. Elife 6 (2017)
...Kim G, Baek J, Park SH, Choi CY, Lee S
RgGuinier 2.7 nm
Dmax 9.4 nm

SASDFD7 – Pseudomonas putida CBB5 NdmAB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 127 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.5 nm
Dmax 12.3 nm

SASDFE7 – Pseudomonas putida CBB5 mCherry-NdmA/NdmB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 207 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 5.4 nm
Dmax 13.8 nm

SASDFF7 – Pseudomonas putida CBB5 NdmA hexamer

Methylxanthine N1-demethylase NdmA experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA hexamer, 254 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.2 nm
Dmax 11.0 nm

SASDFG7 – Pseudomonas putida CBB5 NdmB hexamer

Methylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N3-demethylase NdmB hexamer, 258 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.3 nm
Dmax 12.2 nm

SASDFH7 – Pseudomonas putida CBB5 NdmAB complex

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 127 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.2 nm
Dmax 10.9 nm

SASDFJ7 – Pseudomonas putida CBB5 mCherry-NdmA/ECFP-NdmB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 207 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 208 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 5.6 nm
Dmax 19.1 nm

SASDHN8 – Human tumor necrosis factor receptor superfamily member 5 (CD40) extracellular domain in complex with human immunoglobulin gamma 1 (IgG1) 341G2 F(ab)

Tumor necrosis factor receptor superfamily member 5Human 341G2 F(ab) experimental SAS data
HADDOCK model
Sample: Tumor necrosis factor receptor superfamily member 5 monomer, 19 kDa Homo sapiens protein
Human 341G2 F(ab) monomer, 73 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Sep 18
Isotype Switching Converts Anti-CD40 Antagonism to Agonism to Elicit Potent Antitumor Activity Cancer Cell (2020)
...Kim J, Inzhelevskaya T, Mockridge C, French R, Duriez P, Douglas L, English V, Verbeek J, White A, Tews I, Glennie M, Cragg M
RgGuinier 3.7 nm
Dmax 13.4 nm
VolumePorod 97 nm3

SASDGN2 – F670E mutated dimeric bifunctional alcohol/aldehyde dehydrogenase

F670E Aldehyde-alcohol dehydrogenase experimental SAS data
SREFLEX model
Sample: F670E Aldehyde-alcohol dehydrogenase dimer, 192 kDa Escherichia coli protein
Buffer: 50 mM HEPES pH 7, 500 mM NaCl, 5% (v/v) glycerol, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Oct 4
Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity. Nat Commun 10(1):4527 (2019)
Kim G, Azmi L, Jang S, Jung T, Hebert H, Roe AJ, Byron O, Song JJ
RgGuinier 5.0 nm
Dmax 17.4 nm
VolumePorod 260 nm3

SASDG76 – Inhibitor of apoptosis-stimulating protein of p53 (iASPP(608-828)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, compact

Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor)Serine/threonine-protein phosphatase PP1-alpha catalytic subunit experimental SAS data
BILBOMD model
Sample: Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) monomer, 25 kDa Homo sapiens protein
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.1 nm
Dmax 11.3 nm
VolumePorod 157 nm3

SASDBV9 – Immunoglobulin domain 4 of Nucleoporin Pom152 (Pom152 Ig-4: amino acids 718-820)

Nucleoporin POM152 experimental SAS data
MODELLER model
Sample: Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 1.8 nm
Dmax 6.7 nm
VolumePorod 18 nm3

SASDG86 – Inhibitor of apoptosis-stimulating protein of p53 (iASPP(608-828)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, extended

Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor)Serine/threonine-protein phosphatase PP1-alpha catalytic subunit experimental SAS data
BILBOMD model
Sample: Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) monomer, 25 kDa Homo sapiens protein
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.4 nm
Dmax 12.2 nm
VolumePorod 180 nm3

SASDBW9 – Immunoglobulin domains 4,5 of Nucleoporin Pom152 (Pom152 Ig-4,5: amino acids 718-920)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 24 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 23 nm3

SASDG66 – Inhibitor of apoptosis-stimulating protein of p53 (iASPP(621-828)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, compact

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitInhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) monomer, 25 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Apr 25
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.0 nm
Dmax 10.9 nm
VolumePorod 116 nm3

SASDBX9 – Immunoglobulin domain 6 of Nucleoporin Pom152 (Pom152 Ig-6: amino acids 919-1020)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 2.8 nm
Dmax 7.9 nm
VolumePorod 57 nm3

SASDG56 – Inhibitor of apoptosis-stimulating protein of p53 (iASPP(621-828)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, extended

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitInhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) monomer, 25 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Apr 25
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.4 nm
Dmax 12.4 nm
VolumePorod 132 nm3

SASDBY9 – Immunoglobulin domains 3,4 of Nucleoporin Pom152 (Pom152 Ig-3,4: amino acids 603-820)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 26 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 28 nm3

SASDBZ9 – Immunoglobulin domains 4,5,6,7 of Nucleoporin Pom152 (Pom152 Ig-4,5,6,7: amino acids 718-1148)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 49 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 4.3 nm
Dmax 15.4 nm
VolumePorod 67 nm3

SASDG96 – Apoptosis-stimulating protein 2 of p53 (ASPP2(905-1128)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, compact

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitApoptosis-stimulating of p53 protein 2 experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Apoptosis-stimulating of p53 protein 2 monomer, 26 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 2.9 nm
Dmax 10.2 nm
VolumePorod 144 nm3

SASDGA6 – Apoptosis-stimulating protein 2 of p53 (ASPP2(905-1128)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, extended

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitApoptosis-stimulating of p53 protein 2 experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Apoptosis-stimulating of p53 protein 2 monomer, 26 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.3 nm
Dmax 11.7 nm
VolumePorod 172 nm3