SASBDB entries for UniProt ID:

SASDDG2 – Glycosylated Human Immunoglobulin G Fc Region

UniProt ID: P01857 (108-329) Glycosylated human immunoglobulin G Fc region
Glycosylated human immunoglobulin G Fc region experimental SAS data
MODELLER model
Sample: Glycosylated human immunoglobulin G Fc region dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM Citrate-Phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering. MAbs (2018)
Yageta S, Imamura H, Shibuya R, Honda S
RgGuinier 2.7 nm
Dmax 10.2 nm
VolumePorod 66 nm3

SASDDH2 – Aglycosylated Human Immunoglobulin G Fc Region

UniProt ID: P01857 (104-330) Aglycosylated human immunoglobulin G Fc region
Aglycosylated human immunoglobulin G Fc region experimental SAS data
MODELLER model
Sample: Aglycosylated human immunoglobulin G Fc region dimer, 51 kDa Homo sapiens protein
Buffer: 20 mM Citrate-Phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering. MAbs (2018)
Yageta S, Imamura H, Shibuya R, Honda S
RgGuinier 2.9 nm
Dmax 9.8 nm
VolumePorod 60 nm3

SASDE99 – Calredoxin with EGTA

UniProt ID: A0A2K3DZB3 (25-357) Calredoxin, Redox protein from Chlamydomonas reinhardtii
Calredoxin, Redox protein from Chlamydomonas reinhardtii experimental SAS data
Calredoxin, Redox protein from Chlamydomonas reinhardtii Kratky plot
Sample: Calredoxin, Redox protein from Chlamydomonas reinhardtii monomer, 40 kDa Chlamydomonas reinhardtii protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM EGTA, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Structural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University on 2015 Nov 17
Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga Chlamydomonas reinhardtii. J Biol Chem (2019)
Charoenwattanasatien R, Zinzius K, Scholz M, Wicke S, Tanaka H, Brandenburg JS, Marchetti GM, Ikegami T, Matsumoto T, Oda T, Sato M, Hippler M, Kurisu G
RgGuinier 2.5 nm
Dmax 8.7 nm
VolumePorod 60 nm3

SASDEA9 – Calredoxin with Calcium

UniProt ID: A0A2K3DZB3 (25-357) Calredoxin, Redox protein from Chlamydomonas reinhardtii
Calredoxin, Redox protein from Chlamydomonas reinhardtii experimental SAS data
Calredoxin, Redox protein from Chlamydomonas reinhardtii Kratky plot
Sample: Calredoxin, Redox protein from Chlamydomonas reinhardtii monomer, 40 kDa Chlamydomonas reinhardtii protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM CaCl2, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Structural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University on 2015 Nov 17
Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga Chlamydomonas reinhardtii. J Biol Chem (2019)
Charoenwattanasatien R, Zinzius K, Scholz M, Wicke S, Tanaka H, Brandenburg JS, Marchetti GM, Ikegami T, Matsumoto T, Oda T, Sato M, Hippler M, Kurisu G
RgGuinier 3.1 nm
Dmax 11.6 nm
VolumePorod 68 nm3

SASDEB9 – Flagellar brake protein YcgR from Escherichia coli

UniProt ID: P76010 (None-None) Flagellar brake protein YcgR
Flagellar brake protein YcgR experimental SAS data
SASREF model
Sample: Flagellar brake protein YcgR monomer, 29 kDa Escherichia coli protein
Buffer: 20 mM HEPES, 150mM NaCl, 10% glycerol,, pH: 7.5
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2016 Jan 4
Structural insights into the mechanism of c-di-GMP-bound YcgR regulating flagellar motility in Escherichia coli. J Biol Chem 295(3):808-821 (2020)
Hou YJ, Yang WS, Hong Y, Zhang Y, Wang DC, Li DF
RgGuinier 2.6 nm
Dmax 9.1 nm
VolumePorod 44 nm3

SASDEC9 – Flagellar brake protein YcgR in complex with c-di-GMP from Escherichia coli

UniProt ID: P76010 (None-None) Flagellar brake protein YcgR in complex with c-di-GMP
Flagellar brake protein YcgR in complex with c-di-GMP experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Flagellar brake protein YcgR in complex with c-di-GMP monomer, 29 kDa Escherichia coli protein
Buffer: 20 mM HEPES, 150mM NaCl, 10% glycerol,, pH: 7.5
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2016 Jan 4
Structural insights into the mechanism of c-di-GMP-bound YcgR regulating flagellar motility in Escherichia coli. J Biol Chem 295(3):808-821 (2020)
Hou YJ, Yang WS, Hong Y, Zhang Y, Wang DC, Li DF
RgGuinier 2.2 nm
Dmax 7.3 nm
VolumePorod 44 nm3

SASDED9 – Relaxase domain of TraI

UniProt ID: Q5EPC7 (None-None) Relaxase (Tra_2) domain of TraI
Relaxase (Tra_2) domain of TraI experimental SAS data
GASBOR model
Sample: Relaxase (Tra_2) domain of TraI monomer, 46 kDa Neisseria gonorrhoeae protein
Buffer: 50 mM TRIS-HCl 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Jul 11
DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island. Nucleic Acids Res 47(15):8136-8153 (2019)
Heilers JH, Reiners J, Heller EM, Golzer A, Smits SHJ, van der Does C
RgGuinier 2.6 nm
Dmax 8.3 nm
VolumePorod 61 nm3

SASDEE9 – TraI_2_C domain of TraI

UniProt ID: Q5EPC7 (674-850) TraI_2_C domain of TraI
TraI_2_C domain of TraI experimental SAS data
GASBOR model
Sample: TraI_2_C domain of TraI monomer, 21 kDa Neisseria gonorrhoeae protein
Buffer: 50 mM TRIS-HCl 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Jul 11
DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island. Nucleic Acids Res 47(15):8136-8153 (2019)
Heilers JH, Reiners J, Heller EM, Golzer A, Smits SHJ, van der Does C
RgGuinier 2.2 nm
Dmax 6.5 nm
VolumePorod 40 nm3

SASDEF9 – TraI of Neisseria gonorrhoeae

UniProt ID: Q5EPC7 (42-850) TraI
TraI experimental SAS data
GASBOR model
Sample: TraI monomer, 91 kDa Neisseria gonorrhoeae protein
Buffer: 50 mM TRIS-HCl 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Mar 5
DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island. Nucleic Acids Res 47(15):8136-8153 (2019)
Heilers JH, Reiners J, Heller EM, Golzer A, Smits SHJ, van der Does C
RgGuinier 7.3 nm
Dmax 31.4 nm
VolumePorod 293 nm3

SASDEL9 – Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex

UniProt ID: P21177 (None-None) Fatty acid oxidation complex subunit alpha

UniProt ID: P21177 (None-None) Fatty acid oxidation complex subunit alpha

UniProt ID: P21151 (None-None) 3-ketoacyl-CoA thiolase FadA (beta subunit)
Fatty acid oxidation complex subunit alphaFatty acid oxidation complex subunit alpha3-ketoacyl-CoA thiolase FadA (beta subunit) experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
3-ketoacyl-CoA thiolase FadA (beta subunit) dimer, 82 kDa Escherichia coli protein
Buffer: 20 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 120 mM KCl, 2.5 mM DTT, pH: 7.2
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 30
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 406 nm3