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SASDFB5 – Phosphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
Resistance to inhibitors of cholinesterase 8 homolog A Kratky plot
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 51 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Apr 24
Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A. Structure (2019)
Zeng B, Mou TC, Doukov TI, Steiner A, Yu W, Papasergi-Scott M, Tall GG, Hagn F, Sprang SR
RgGuinier 3.0 nm
Dmax 10.1 nm
VolumePorod 70 nm3

SASDF52 – dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE

Dosage compensation regulator experimental SAS data
dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE Rg histogram
Sample: Dosage compensation regulator monomer, 29 kDa Drosophila melanogaster protein
Buffer: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 29
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res 47(8):4319-4333 (2019)
Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 22 nm3

SASDEF5 – Phosphoketolase (L. lactis) with 1 mM thiaminpyrophosphate and 2% v/v glycerol at pH 7.0

Probable phosphoketolase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Probable phosphoketolase dimer, 191 kDa Lactococcus lactis subsp. … protein
Buffer: 20mM potassium phosphate 150mM NaCl 0.007 %(w/v) β-octyl glucoside 1mM DTT 1mM MgCl 1mM thiaminpyrophosphate 2 %(v/v) glycerol, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 7
Crystal structure of a xylulose 5-phosphate phosphoketolase. insights into the substrate specificity for xylulose 5-phosphate. J Struct Biol (2019)
Scheidig AJ, Horvath D, Szedlacsek SE
RgGuinier 3.4 nm
Dmax 10.2 nm
VolumePorod 237 nm3

SASDEB8 – Bacillus thuringiensis LexA repressor (Bt_LexA)

Bacillus thuringiensis LexA repressor experimental SAS data
CHIMERA model
Sample: Bacillus thuringiensis LexA repressor dimer, 47 kDa Bacillus thuringiensis protein
Buffer: 20 mM Hepes, 300 mM NaCl, 10% glycerol,, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-2000, University of British Columbia on 2017 Aug 25
Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor. Structure 27(7):1094-1102.e4 (2019)
Caveney NA, Pavlin A, Caballero G, Bahun M, Hodnik V, de Castro L, Fornelos N, Butala M, Strynadka NCJ
RgGuinier 3.7 nm
VolumePorod 110 nm3

SASDEC8 – Bacillus thuringiensis LexA repressor bound to Bacteriophage pGIL01 gp7 (Bt_LexA_GIL01_gp7)

Bacillus thuringiensis LexA repressorBacteriophage pGIL01 gp7 experimental SAS data
CHIMERA model
Sample: Bacillus thuringiensis LexA repressor dimer, 47 kDa Bacillus thuringiensis protein
Bacteriophage pGIL01 gp7 tetramer, 24 kDa Bacteriophage pGIL01 protein
Buffer: 20 mM Hepes, 300 mM NaCl, 10% glycerol,, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-2000, University of British Columbia on 2017 Aug 25
Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor. Structure 27(7):1094-1102.e4 (2019)
Caveney NA, Pavlin A, Caballero G, Bahun M, Hodnik V, de Castro L, Fornelos N, Butala M, Strynadka NCJ
RgGuinier 4.4 nm

SASDC45 – Alpha domain of autotransporter protein UpaB from UPEC

Alpha domain of autotransporter protein UpaB experimental SAS data
CORAL model
Sample: Alpha domain of autotransporter protein UpaB monomer, 48 kDa E. Coli CFT073 protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 May 1
Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules. Nat Commun 10(1):1967 (2019)
Paxman JJ, Lo AW, Sullivan MJ, Panjikar S, Kuiper M, Whitten AE, Wang G, Luan CH, Moriel DG, Tan L, Peters KM, Phan MD, Gee CL, Ulett GC, Schembri MA, Heras B
RgGuinier 2.9 nm
Dmax 10.5 nm
VolumePorod 66 nm3

SASDDH9 – Chloroplastic phosphoribulokinase (collected using SEC-SAXS)

Phosphoribulokinase, chloroplastic experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Phosphoribulokinase, chloroplastic dimer, 78 kDa Chlamydomonas reinhardtii protein
Buffer: Tris-HCl 50 mM 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 15
Arabidopsis and Chlamydomonas phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle. Proc Natl Acad Sci U S A 116(16):8048-8053 (2019)
Gurrieri L, Del Giudice A, Demitri N, Falini G, Pavel NV, Zaffagnini M, Polentarutti M, Crozet P, Marchand CH, Henri J, Trost P, Lemaire SD, Sparla F, Fermani S
RgGuinier 3.4 nm
Dmax 11.3 nm
VolumePorod 115 nm3

SASDFS4 – HP0242 from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, de novo designed coiled-coil trimer domain (Domain A (PDB:3MLI)-Linker (PDB:1BR0)-Domain B (PDB:4DZL))

HP0242 from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, de novo designed coiled-coil trimer domain experimental SAS data
CORAL model
Sample: HP0242 from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, de novo designed coiled-coil trimer domain hexamer, 179 kDa Helicobacter pylori, Rattus … protein
Buffer: 20 mM Tris-HCl 150 mM NaCl, pH: 8
Experiment: SAXS data collected at Rigaku Nano-Viewer, Nara Institute of Science and Technology on 2017 Mar 29
Construction of a Quadrangular Tetramer and a Cage-Like Hexamer from Three-Helix Bundle-Linked Fusion Proteins. ACS Synth Biol (2019)
Miyamoto T, Hayashi Y, Yoshida K, Watanabe H, Uchihashi T, Yonezawa K, Shimizu N, Kamikubo H, Hirota S
RgGuinier 6.5 nm
Dmax 24.0 nm
VolumePorod 642 nm3

SASDE66 – C. limicola ATP-citrate lyase (ACL) in HBS

ATP-citrate lyase experimental SAS data
ATP-citrate lyase Kratky plot
Sample: ATP-citrate lyase tetramer, 429 kDa Chlorobium limicola protein
Buffer: 20mM HEPES, 150mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 6.1 nm
Dmax 20.0 nm
VolumePorod 666 nm3

SASDE76 – C. limicola ATP-citrate lyase (ACL) in HBS + Citrate

ATP-citrate lyase experimental SAS data
ATP-citrate lyase Kratky plot
Sample: ATP-citrate lyase tetramer, 429 kDa Chlorobium limicola protein
Buffer: 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 6.0 nm
Dmax 20.0 nm
VolumePorod 672 nm3