SASBDB entries for UniProt ID:

SASDBR6 – Nucleolysin TIA-1 isoform p40 in complex with UUUUUACUCC RNA

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

UniProt ID: (None-None) RNA (UUUUUACU)
Nucleolysin TIA-1 isoform p40RNA (UUUUUACU) experimental SAS data
Nucleolysin TIA-1 isoform p40 RNA (UUUUUACU) Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
RNA (UUUUUACU) 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 2.1 nm
Dmax 6.5 nm
VolumePorod 26 nm3

SASDBD7 – Human Proliferating Cell Nuclear Antigen (PCNA)

UniProt ID: P12004 (None-None) Proliferating cell nuclear antigen
Proliferating cell nuclear antigen experimental SAS data
GASBOR model
Sample: Proliferating cell nuclear antigen trimer, 89 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 9.7 nm
VolumePorod 128 nm3

SASDBH7 – Dps1 truncated, DNA binding protein under starvation conditions (SEC-SAXS)

UniProt ID: Q9RS64 (51-207) N-terminal truncated DNA protection during starvation protein 1
N-terminal truncated DNA protection during starvation protein 1 experimental SAS data
GASBOR model
Sample: N-terminal truncated DNA protection during starvation protein 1 dodecamer, 216 kDa Deinococcus radiodurans R1 protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV
RgGuinier 3.9 nm
Dmax 10.0 nm
VolumePorod 291 nm3

SASDB58 – Major viral transcription factor ICP4 (ICP4N dimer)

UniProt ID: P08392 (258-487) Major viral transcription factor ICP4
Major viral transcription factor ICP4 experimental SAS data
Major viral transcription factor ICP4 Kratky plot
Sample: Major viral transcription factor ICP4 dimer, 49 kDa Human alphaherpesvirus 1 protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2015 Jul 27
The herpes viral transcription factor ICP4 forms a novel DNA recognition complex. Nucleic Acids Res 45(13):8064-8078 (2017)
Tunnicliffe RB, Lockhart-Cairns MP, Levy C, Mould AP, Jowitt TA, Sito H, Baldock C, Sandri-Goldin RM, Golovanov AP
RgGuinier 2.9 nm
Dmax 12.7 nm

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

UniProt ID: P39685 (None-None) Nucleoporin POM152
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)
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 2.7 nm
Dmax 9.4 nm
VolumePorod 23 nm3

SASDC72 – Alcohol dehydrogenase from bifunctional alcohol/aldehyde dehydrogenase (P0A9Q8)

UniProt ID: P0A9Q8 (451-891) Aldehyde-alcohol dehydrogenase
Aldehyde-alcohol dehydrogenase experimental SAS data
DAMMIF model
Sample: Aldehyde-alcohol dehydrogenase dimer, 97 kDa Escherichia coli O157:H7 protein
Buffer: 20 mM Tris 400 mM NaCl 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2015 Nov 27
High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE. Acta Crystallogr F Struct Biol Commun 76(Pt 9):414-421 (2020)
Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M
RgGuinier 3.2 nm
Dmax 16.9 nm
VolumePorod 146 nm3

SASDCS2 – Bromodomain-containing protein 3 (BRD3) tandem bromodomains

UniProt ID: Q15059 (20-418) Bromodomain-containing protein 3
Bromodomain-containing protein 3 experimental SAS data
DAMMIN model
Sample: Bromodomain-containing protein 3 monomer, 44 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 6.2 nm
Dmax 21.5 nm
VolumePorod 210 nm3

SASDD63 – Collagenase ColG s2s3as3b at pCa 3 (second analysis)

UniProt ID: Q9X721 (787-1118) Collagenase ColG segement s2s3as3b
Collagenase ColG segement s2s3as3b experimental SAS data
DAMFILT 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 11
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 3.0 nm
Dmax 14.4 nm
VolumePorod 61 nm3

SASDDN9 – Mycobacterium tuberculosis DNA Ligase A

UniProt ID: P9WNV1 (1-691) DNA ligase A
DNA ligase A experimental SAS data
DAMFILT model
Sample: DNA ligase A monomer, 76 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 5.2 nm
Dmax 16.7 nm
VolumePorod 870 nm3

SASDDP9 – C-terminal half of pseudorabies virus tegument protein UL37

UniProt ID: Q911W0 (478-919) Tegument protein UL37
Tegument protein UL37 experimental SAS data
DAMMIN model
Sample: Tegument protein UL37 monomer, 49 kDa Suid alphaherpesvirus 1 protein
Buffer: 100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 3
The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 293(41):15827-15839 (2018)
Koenigsberg AL, Heldwein EE
RgGuinier 4.2 nm
Dmax 14.0 nm
VolumePorod 71 nm3