SASBDB entries for UniProt ID:

SASDBQ9 – Human Hsp90 co-chaperone Cdc37 (CD37) in complex with fibroblast growth factor receptor 3

UniProt ID: Q16543 (None-None) Hsp90 co-chaperone Cdc37

UniProt ID: P22607 (455-768) Fibroblast growth factor receptor 3
Hsp90 co-chaperone Cdc37Fibroblast growth factor receptor 3 experimental SAS data
CORAL model
Sample: Hsp90 co-chaperone Cdc37 monomer, 44 kDa Homo sapiens protein
Fibroblast growth factor receptor 3 monomer, 35 kDa Homo sapiens protein
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jul 10
Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System. Structure 26(3):446-458.e8 (2018)
Bunney TD, Inglis AJ, Sanfelice D, Farrell B, Kerr CJ, Thompson GS, Masson GR, Thiyagarajan N, Svergun DI, Williams RL, Breeze AL, Katan M
RgGuinier 4.7 nm
Dmax 19.5 nm
VolumePorod 161 nm3

SASDBR9 – Human fibroblast growth factor receptor 3, from SEC-SAXS

UniProt ID: P22607 (455-768) Fibroblast growth factor receptor 3
Fibroblast growth factor receptor 3 experimental SAS data
CORAL model
Sample: Fibroblast growth factor receptor 3 monomer, 35 kDa Homo sapiens protein
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jul 10
Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System. Structure 26(3):446-458.e8 (2018)
Bunney TD, Inglis AJ, Sanfelice D, Farrell B, Kerr CJ, Thompson GS, Masson GR, Thiyagarajan N, Svergun DI, Williams RL, Breeze AL, Katan M
RgGuinier 2.4 nm
Dmax 8.3 nm
VolumePorod 59 nm3

SASDBT9 – Full-length human βB2-crystallin

UniProt ID: P43320 (None-None) Beta-crystallin B2
Beta-crystallin B2 experimental SAS data
DAMMIN model
Sample: Beta-crystallin B2 dimer, 46 kDa Homo sapiens protein
Buffer: 25 mM NaPi, 5 mM DTT, 1 mM EDTA,, pH: 6.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Mar 20
Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Structure 25(3):496-505 (2017)
Xi Z, Whitley MJ, Gronenborn AM
RgGuinier 2.2 nm
Dmax 8.1 nm
VolumePorod 67 nm3

SASDBU9 – Terminally truncated human βB2-crystallin

UniProt ID: P43320 (15-195) Beta-crystallin B2
Beta-crystallin B2 experimental SAS data
DAMMIN model
Sample: Beta-crystallin B2 dimer, 42 kDa Homo sapiens protein
Buffer: 25 mM NaPi, 5 mM DTT, 1 mM EDTA,, pH: 6.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Mar 20
Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Structure 25(3):496-505 (2017)
Xi Z, Whitley MJ, Gronenborn AM
RgGuinier 2.1 nm
Dmax 6.7 nm
VolumePorod 62 nm3

SASDC22 – Tandem LIM domains of the neuronal transcription factor homeobox protein CEH-14 fused to the LIM interaction domain of ceLIM-7

UniProt ID: P20271 (42-168) Homeobox protein CEH-14

UniProt ID: G5EC36 (347-376) CeLIM-7
Homeobox protein CEH-14CeLIM-7 experimental SAS data
DAMMIN model
Sample: Homeobox protein CEH-14 monomer, 16 kDa Caenorhabditis elegans protein
CeLIM-7 monomer, 4 kDa Caenorhabditis elegans protein
Buffer: 50 mM Tris, 100 mM NaCl, 5 mM TCEP, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSess, University of Sydney on 2009 Apr 7
Interactions between LHX3- and ISL1-family LIM-homeodomain transcription factors are conserved in Caenorhabditis elegans. Sci Rep 7(1):4579 (2017)
Bhati M, Llamosas E, Jacques DA, Jeffries CM, Dastmalchi S, Ripin N, Nicholas HR, Matthews JM
RgGuinier 2.4 nm
Dmax 8.9 nm
VolumePorod 26 nm3

SASDC32 – Ethylene Receptor 1 Cytosolic Domain (in 250 mM NDSB)

UniProt ID: P49333 (158-738) Ethylene Receptor 1
Ethylene Receptor 1 experimental SAS data
Ethylene Receptor 1 Cytosolic Domain (in 250 mM NDSB) Rg histogram
Sample: Ethylene Receptor 1 dimer, 129 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris-NDSB 150 mM NaCl 1mM DTT 250 mM NDSB, pH: 8.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 19
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 4.7 nm
Dmax 15.8 nm
VolumePorod 316 nm3

SASDC42 – Ethylene Receptor 1 Cytosolic Domain

UniProt ID: P49333 (158-738) Ethylene Receptor 1
Ethylene Receptor 1 experimental SAS data
Ethylene Receptor 1 Cytosolic Domain Rg histogram
Sample: Ethylene Receptor 1 dimer, 129 kDa Arabidopsis thaliana protein
Buffer: 20 mM TRIS 150 mM NaCl 1mM DTT 250mM NDSB, pH: 8.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Mar 29
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 5.5 nm
Dmax 19.0 nm
VolumePorod 274 nm3

SASDC52 – Bruton tyrosine kinase

UniProt ID: Q06187 (None-None) Tyrosine-protein kinase BTK (R28C mutant)
Tyrosine-protein kinase BTK (R28C mutant) experimental SAS data
GASBOR model
Sample: Tyrosine-protein kinase BTK (R28C mutant) monomer, 76 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl, 2 mM DTT and 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2002 Apr 2
Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering. EMBO J 22(18):4616-24 (2003)
Márquez JA, Smith CI, Petoukhov MV, Lo Surdo P, Mattsson PT, Knekt M, Westlund A, Scheffzek K, Saraste M, Svergun DI
RgGuinier 5.0 nm
Dmax 20.0 nm
VolumePorod 130 nm3

SASDC62 – Basic domain of telomeric repeat-binding factor 2 (TRF2)

UniProt ID: Q15554 (42-86) Basic domain of telomeric repeat-binding factor 2
Basic domain of telomeric repeat-binding factor 2 experimental SAS data
Basic domain of telomeric repeat-binding factor 2 Kratky plot
Sample: Basic domain of telomeric repeat-binding factor 2 monomer, 5 kDa Homo sapiens protein
Buffer: 50 mM NaPi, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2015 Mar 5
Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it. Nucleic Acids Res 45(21):12170-12180 (2017)
Necasová I, Janoušková E, Klumpler T, Hofr C
RgGuinier 1.7 nm
Dmax 7.1 nm
VolumePorod 4 nm3

SASDC82 – Rab family protein CtRoco nucleotide free

UniProt ID: Q8KC98 (1-1102) Rab family protein
Rab family protein experimental SAS data
DAMMIN model
Sample: Rab family protein dimer, 254 kDa Chlorobaculum tepidum protein
Buffer: 20 mM HEPES 150 mM NaCl 5 mM MgCl2 5% Glycerol 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Feb 16
A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. Nat Commun 8(1):1008 (2017)
Deyaert E, Wauters L, Guaitoli G, Konijnenberg A, Leemans M, Terheyden S, Petrovic A, Gallardo R, Nederveen-Schippers LM, Athanasopoulos PS, Pots H, Van Haastert PJM, Sobott F, Gloeckner CJ, Efremov R, Kortholt A, Versées W
RgGuinier 5.0 nm
Dmax 18.4 nm
VolumePorod 440 nm3