SASBDB entries for UniProt ID:

SASDB46 – Glycosylated Myelin-associated glycoprotein immunoglobulin domains 1-3

UniProt ID: P20917 (20-325) Myelin-associated glycoprotein Ig domains 1-3
Myelin-associated glycoprotein Ig domains 1-3 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein Ig domains 1-3 monomer, 35 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 59 nm3

SASDBK6 – Truncated construct of human p23 (1-131)

UniProt ID: Q15185 (1-131) Prostaglandin E synthase 3 (1-131)
Prostaglandin E synthase 3 (1-131) experimental SAS data
Prostaglandin E synthase 3 (1-131) Kratky plot
Sample: Prostaglandin E synthase 3 (1-131) monomer, 16 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 21
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 31 nm3

SASDBN6 – Nucleolysin TIA-1 isoform p40 in complex with ACUCCUUUUU RNA

UniProt ID: P31483-2 (93-274) Nucleolysin TIA-1 isoform p40

UniProt ID: (None-None) RNA (ACUCCUUUUU)
Nucleolysin TIA-1 isoform p40RNA (ACUCCUUUUU) experimental SAS data
Nucleolysin TIA-1 isoform p40 RNA (ACUCCUUUUU) Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
RNA (ACUCCUUUUU) monomer, 1 kDa RNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 May 27
TIA-1 RRM23 binding and recognition of target oligonucleotides. Nucleic Acids Res 45(8):4944-4957 (2017)
Waris S, García-Mauriño SM, Sivakumaran A, Beckham SA, Loughlin FE, Gorospe M, Díaz-Moreno I, Wilce MCJ, Wilce JA
RgGuinier 2.2 nm
Dmax 6.6 nm
VolumePorod 30 nm3

SASDBA7 – Human NEI like DNA glycosylase 1 (NEIL1) bound to Proliferating Cell Nuclear Antigen (PCNA) and DNA

UniProt ID: Q96FI4 (None-None) Endonuclease 8-like 1

UniProt ID: (None-None) dsDNA

UniProt ID: P12004 (None-None) Proliferating cell nuclear antigen
Endonuclease 8-like 1dsDNAProliferating cell nuclear antigen experimental SAS data
DAMMIN model
Sample: Endonuclease 8-like 1 monomer, 45 kDa Homo sapiens protein
DsDNA monomer, 2 kDa DNA
Proliferating cell nuclear antigen monomer, 30 kDa Homo sapiens protein
Buffer: 25mM HEPES 100mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jan 20
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 45(5):2897-2909 (2017)
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.4 nm
Dmax 16.4 nm
VolumePorod 113 nm3

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

UniProt ID: P39685 (None-None) Nucleoporin POM152
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)
Upla P, 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

SASDCU2 – Bromodomain testis-specific protein (BRDT) tandem bromodomains

UniProt ID: Q58F21 (9-379) Bromodomain testis-specific protein
Bromodomain testis-specific protein experimental SAS data
DAMMIN model
Sample: Bromodomain testis-specific protein monomer, 43 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2% glycerol, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Jan 13
Interactome Rewiring Following Pharmacological Targeting of BET Bromodomains. Mol Cell (2018)
Lambert JP, Picaud S, Fujisawa T, Hou H, Savitsky P, Uusküla-Reimand L, Gupta GD, Abdouni H, Lin ZY, Tucholska M, Knight JDR, Gonzalez-Badillo B, St-Denis N, Newman JA, Stucki M, Pelletier L, Bandeira N, Wilson MD, Filippakopoulos P, Gingras AC
RgGuinier 5.1 nm
Dmax 20.0 nm
VolumePorod 200 nm3

SASDCU4 – Collagenase ColG s2s3as3b at pCa 5

UniProt ID: Q9X721 (787-1118) Collagenase ColG segement s2s3as3b
Collagenase ColG segement s2s3as3b experimental SAS data
DAMMIF model
Sample: Collagenase ColG segement s2s3as3b monomer, 37 kDa Hathewaya histolytica protein
Buffer: 10mM HEPES 100mM NaCl 0.2mM EGTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ - Induced Structural Change of Multi-Domain Collagen Binding Segments of Collagenases ColG and ColH from Hathewaya histolytica University of Arkansas Dissertation - (2018)
Christopher E Ruth
RgGuinier 4.3 nm
Dmax 19.7 nm
VolumePorod 98 nm3

SASDEW3 – DNA ligase A (MtbLigA) complexed with exodeoxyribonuclease III protein (MtbXthA)

UniProt ID: P9WNV1 (None-None) DNA ligase A

UniProt ID: A0A0T9L251 (1-291) Probable exodeoxyribonuclease III protein XthA
DNA ligase AProbable exodeoxyribonuclease III protein XthA experimental SAS data
DAMMIF model
Sample: DNA ligase A monomer, 76 kDa Mycobacterium tuberculosis protein
Probable exodeoxyribonuclease III protein XthA monomer, 33 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 13
M. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair. Nucleic Acids Res (2020)
Khanam T, Afsar M, Shukla A, Alam F, Kumar S, Soyar H, Dolma K, Pasupuleti M, Srivastava KK, Ampapathi RS, Ramachandran R
RgGuinier 6.2 nm
Dmax 23.9 nm
VolumePorod 662 nm3

SASDEZ5 – Albumin-insulin detemir 2:12 complex, P2 symmetry

UniProt ID: P02768 (25-609) Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)

UniProt ID: P01308 (None-None) Insulin detemir (Levemir(R), Novo Nordisk A/S)
Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)Insulin detemir (Levemir(R), Novo Nordisk A/S) experimental SAS data
SASREF CV model
Sample: Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) monomer, 66 kDa protein
Insulin detemir (Levemir(R), Novo Nordisk A/S) dodecamer, 71 kDa protein
Buffer: 8.8 mM Na2HPO4, 10.6 mM m-cresol, 12.2 mM phenol, 140.9 mM glycerol, 56.9 mM NaCl, pH: 7.4
Experiment: SAXS data collected at I911-4, MAX IV on 2015 Sep 25
Solution structures of long-acting insulin analogues and their complexes with albumin. Acta Crystallogr D Struct Biol 75(Pt 3):272-282 (2019)
Ryberg LA, Sønderby P, Barrientos F, Bukrinski JT, Peters GHJ, Harris P
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 309 nm3

SASDET7 – Stator protein complex FlaG-V118K/FlaF

UniProt ID: Q4J9K8 (35-164) Conserved flagellar protein F

UniProt ID: Q4J9K7 (32-151) Stator protein FlaG-V118K soluble domain
Conserved flagellar protein FStator protein FlaG-V118K soluble domain experimental SAS data
MULTIFOXS model
Sample: Conserved flagellar protein F dimer, 32 kDa Sulfolobus acidocaldarius protein
Stator protein FlaG-V118K soluble domain dimer, 30 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 108 nm3