Browse by ORGANISM: other species

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

SASDEJ7 – The InvC-ATP synthase, surface presentation of antigens and oxygen-regulated invasion protein (ISO) complex

Surface presentation of antigens protein SpaO SpaO(SPOA2)Surface presentation of antigens protein SpaO(SPOA1,2)Oxygen-regulated invasion protein OrgBATP synthase  InvC experimental SAS data
Surface presentation of antigens protein SpaO SpaO(SPOA2) Surface presentation of antigens protein SpaO(SPOA1,2) Oxygen-regulated invasion protein OrgB ATP synthase  InvC Kratky plot
Sample: Surface presentation of antigens protein SpaO SpaO(SPOA2) dimer, 25 kDa Salmonella enterica subsp. … protein
Surface presentation of antigens protein SpaO(SPOA1,2) monomer, 34 kDa Salmonella enterica subsp. … protein
Oxygen-regulated invasion protein OrgB dimer, 53 kDa Salmonella enterica subsp. … protein
ATP synthase InvC monomer, 48 kDa Salmonella enterica subsp. … protein
Buffer: 10 mM Tris-HCl, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Apr 12
Molecular Organization of Soluble Type III Secretion System Sorting Platform Complexes. J Mol Biol 431(19):3787-3803 (2019)
Bernal I, Börnicke J, Heidemann J, Svergun D, Horstmann JA, Erhardt M, Tuukkanen A, Uetrecht C, Kolbe M
RgGuinier 6.0 nm
Dmax 22.7 nm
VolumePorod 302 nm3

SASDEK7 – SpaO C-terminus

Surface presentation of antigens protein SpaO(SPOA1,2) C-terminus experimental SAS data
Surface presentation of antigens protein SpaO(SPOA1,2) C-terminus Kratky plot
Sample: Surface presentation of antigens protein SpaO(SPOA1,2) C-terminus monomer, 19 kDa Salmonella enterica subsp. … protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Apr 24
Molecular Organization of Soluble Type III Secretion System Sorting Platform Complexes. J Mol Biol 431(19):3787-3803 (2019)
Bernal I, Börnicke J, Heidemann J, Svergun D, Horstmann JA, Erhardt M, Tuukkanen A, Uetrecht C, Kolbe M
RgGuinier 2.1 nm
Dmax 7.2 nm

SASDFC6 – Wild type protein kinase YopO

Protein kinase YopO experimental SAS data
CUSTOM IN-HOUSE model
Sample: Protein kinase YopO monomer, 63 kDa Yersinia enterocolitica protein
Buffer: 10 mM Tris-HCl, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 May 6
Studying Conformational Changes of the Yersinia Type-III-Secretion Effector YopO in Solution by Integrative Structural Biology. Structure 27(9):1416-1426.e3 (2019)
Peter MF, Tuukkanen AT, Heubach CA, Selsam A, Duthie FG, Svergun DI, Schiemann O, Hagelueken G
RgGuinier 3.3 nm
Dmax 11.5 nm
VolumePorod 119 nm3

SASDES6 – The 11S subunit of the Plasmodium falciparum proteasome, PA28

Proteasome activator PA28 experimental SAS data
CORAL model
Sample: Proteasome activator PA28 heptamer, 232 kDa Plasmodium falciparum protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 0.5 mM TCEP, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Dec 2
The structure of the PA28-20S proteasome complex from Plasmodium falciparum and implications for proteostasis. Nat Microbiol 4(11):1990-2000 (2019)
Xie SC, Metcalfe RD, Hanssen E, Yang T, Gillett DL, Leis AP, Morton CJ, Kuiper MJ, Parker MW, Spillman NJ, Wong W, Tsu C, Dick LR, Griffin MDW, Tilley L
RgGuinier 4.3 nm
Dmax 12.9 nm
VolumePorod 484 nm3

SASDDE7 – Class I chitinase 1 from Agave tequilana

Chitinase 1 experimental SAS data
DAMMIF model
Sample: Chitinase 1 monomer, 32 kDa Agave tequilana protein
Buffer: MES 50 mM, pH: 6
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2017 Apr 26
A biophysical and structural study of two chitinases from Agave tequilana and their potential role as defense proteins. FEBS J (2019)
Sierra-Gómez Y, Rodríguez-Hernández A, Cano-Sánchez P, Gómez-Velasco H, Hernández-Santoyo A, Siliqi D, Rodríguez-Romero A
RgGuinier 2.6 nm
Dmax 9.7 nm
VolumePorod 52 nm3

SASDDA6 – Class I chitinase 2 from Agave tequilana

Chitinase 2 experimental SAS data
DAMMIF model
Sample: Chitinase 2 monomer, 32 kDa Agave tequilana protein
Buffer: MES 50 mM, pH: 6
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2017 Apr 19
A biophysical and structural study of two chitinases from Agave tequilana and their potential role as defense proteins. FEBS J (2019)
Sierra-Gómez Y, Rodríguez-Hernández A, Cano-Sánchez P, Gómez-Velasco H, Hernández-Santoyo A, Siliqi D, Rodríguez-Romero A
RgGuinier 2.4 nm
Dmax 9.8 nm
VolumePorod 49 nm3