Small Angle Scattering Biological Data Bank SASBDB

Browse by MACROMOLECULE type: protein

SASDCT8 – Uncharacterized protein CTHT_0072540 (Core) from Chaetomium thermophilum

hypothetical protein CTHT_0072540 experimental SAS data

Sample:	Hypothetical protein CTHT_0072540 tetramer, 62 kDa Chaetomium thermophilum protein
Buffer:	20 mM HEPES, 100 mM NaCl, 2 mM β-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Jul 30

Prp19/Pso4 Is an Autoinhibited Ubiquitin Ligase Activated by Stepwise Assembly of Three Splicing Factors. Mol Cell 69(6):979-992.e6 (2018)
de Moura TR, Mozaffari-Jovin S, Szabó CZK, Schmitzová J, Dybkov O, Cretu C, Kachala M, Svergun D, Urlaub H, Lührmann R, Pena V

R_g^Guinier	4.1	nm
D_max	16.2	nm
Volume^Porod	145	nm³

SASDCU8 – Uncharacterized protein CTHT_0072540 (WD40) from Chaetomium thermophilum

Sample:	Hypothetical protein CTHT_0072540 monomer, 35 kDa Chaetomium thermophilum protein
Buffer:	20 mM HEPES, 100 mM NaCl, 2 mM β-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Jul 19

R_g^Guinier	2.3	nm
D_max	5.8	nm
Volume^Porod	68	nm³

SASDCV8 – Uncharacterized protein CTHT_0072540 (Prp19 full-length) from Chaetomium thermophilum

Full-length hypothetical protein CTHT_0072540 experimental SAS data

Sample:	Full-length hypothetical protein CTHT_0072540 tetramer, 207 kDa Chaetomium thermophilum protein
Buffer:	20 mM HEPES, 100 mM NaCl, 2 mM β-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at I911-4, MAX IV on 2013 Oct 15

R_g^Guinier	6.2	nm
D_max	23.0	nm
Volume^Porod	280	nm³

SASDC57 – Deoxyuridine 5'-triphosphate nucleotidohydrolase

Deoxyuridine 5'-triphosphate nucleotidohydrolase experimental SAS data

Sample:	Deoxyuridine 5'-triphosphate nucleotidohydrolase trimer, 54 kDa Homo sapiens protein
Buffer:	50 mM HEPES 300 mM NaCl 5 mM MgCl2, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2016 Jul 9

Structural model of human dUTPase in complex with a novel proteinaceous inhibitor. Sci Rep 8(1):4326 (2018)
Nyíri K, Mertens HDT, Tihanyi B, Nagy GN, Kőhegyi B, Matejka J, Harris MJ, Szabó JE, Papp-Kádár V, Németh-Pongrácz V, Ozohanics O, Vékey K, Svergun DI, Borysik AJ, Vértessy BG

R_g^Guinier	3.0	nm
D_max	10.0	nm
Volume^Porod	117	nm³

SASDC67 – SaPIbov1 pathogenicity island repressor

SaPIbov1 pathogenicity island repressor experimental SAS data

Sample:	SaPIbov1 pathogenicity island repressor dimer, 64 kDa Staphylococcus aureus protein
Buffer:	50 mM HEPES 300 mM NaCl 5 mM MgCl2, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2016 Jul 9

R_g^Guinier	3.3	nm
D_max	10.5	nm
Volume^Porod	100	nm³

SASDC77 – Deoxyuridine 5'-triphosphate nucleotidohydrolase complex with SaPIbov1 pathogenicity island repressor [3:3] (SEC-SAXS)

Deoxyuridine 5'-triphosphate nucleotidohydrolaseSaPIbov1 pathogenicity island repressor experimental SAS data

Sample:	Deoxyuridine 5'-triphosphate nucleotidohydrolase trimer, 54 kDa Homo sapiens protein SaPIbov1 pathogenicity island repressor dimer, 64 kDa Staphylococcus aureus protein
Buffer:	50 mM HEPES 300 mM NaCl 5 mM MgCl2, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2016 Jul 10

R_g^Guinier	4.4	nm
D_max	17.0	nm
Volume^Porod	227	nm³

SASDC87 – Deoxyuridine 5'-triphosphate nucleotidohydrolase complex with SaPIbov1 pathogenicity island repressor [3:2] (SEC-SAXS)

Sample:	Deoxyuridine 5'-triphosphate nucleotidohydrolase trimer, 54 kDa Homo sapiens protein SaPIbov1 pathogenicity island repressor dimer, 64 kDa Staphylococcus aureus protein
Buffer:	50 mM HEPES 300 mM NaCl 5 mM MgCl2, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2016 Jul 10

R_g^Guinier	3.8	nm
D_max	14.0	nm
Volume^Porod	190	nm³

SASDBP9 – Human Hsp90 co-chaperone Cdc37 protein (CD37)

Hsp90 co-chaperone Cdc37 experimental SAS data

Sample:	Hsp90 co-chaperone Cdc37 monomer, 44 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

R_g^Guinier	4.0	nm
D_max	15.5	nm
Volume^Porod	106	nm³

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

Hsp90 co-chaperone Cdc37Fibroblast growth factor receptor 3 experimental SAS data

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

R_g^Guinier	4.7	nm
D_max	19.5	nm
Volume^Porod	161	nm³

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

Fibroblast growth factor receptor 3 experimental SAS data

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

R_g^Guinier	2.4	nm
D_max	8.3	nm
Volume^Porod	59	nm³

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