Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Ab initio only

SASDAJ4 – CRM1

Sample:	Exportin-1 monomer, 123 kDa Mus musculus protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3

Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A

R_g^Guinier	3.8	nm
D_max	11.0	nm
Volume^Porod	190	nm³

SASDAK4 – CRM1 RanGTP

Exportin-1GTP-binding nuclear protein Ran experimental SAS data

Sample:	Exportin-1 monomer, 123 kDa Mus musculus protein GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3

R_g^Guinier	3.6	nm
D_max	10.0	nm

SASDAL4 – CRM1 RanGTP Snu1

Exportin-1GTP-binding nuclear protein RanSnurportin-1 experimental SAS data

Sample:	Exportin-1 monomer, 123 kDa Mus musculus protein GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein Snurportin-1 monomer, 41 kDa Homo sapiens protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3

R_g^Guinier	4.1	nm
D_max	14.0	nm

SASDAM4 – CRM1 Snu1

Exportin-1Snurportin-1 experimental SAS data

Sample:	Exportin-1 monomer, 123 kDa Mus musculus protein Snurportin-1 monomer, 41 kDa Homo sapiens protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 10

R_g^Guinier	4.3	nm
D_max	15.0	nm

SASDLV4 – Ceruloplasmin ternary complex with lactoferrin and myeloperoxidase

CeruloplasminLactotransferrinMyeloperoxidase experimental SAS data

Sample:	Ceruloplasmin dimer, 244 kDa Homo sapiens protein Lactotransferrin dimer, 156 kDa Homo sapiens protein Myeloperoxidase dimer, 132 kDa Homo sapiens protein
Buffer:	0.1 M sodium-acetate buffer, pH: 5.6
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24

Ceruloplasmin: Macromolecular Assemblies with Iron-Containing Acute Phase Proteins PLoS ONE 8(7):e67145 (2013)
Samygina V, Sokolov A, Bourenkov G, Petoukhov M, Pulina M, Zakharova E, Vasilyev V, Bartunik H, Svergun D, Tuma R

R_g^Guinier	6.9	nm
D_max	22.6	nm
Volume^Porod	726	nm³

SASDA85 – CHD4 (PP-CC-AH-D)

Human Chromatin Remodeler CHD4 (363-1353) experimental SAS data

Sample:	Human Chromatin Remodeler CHD4 (363-1353) monomer, 117 kDa Homo sapiens protein
Buffer:	50 mM HEPES 5% Glycerol 300 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 13

The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. J Mol Biol 422(1):3-17 (2012)
Watson AA, Mahajan P, Mertens HD, Deery MJ, Zhang W, Pham P, Du X, Bartke T, Zhang W, Edlich C, Berridge G, Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, Laue ED

R_g^Guinier	4.9	nm
D_max	17.4	nm

SASDA95 – CHD4 (CC-AH-D)

Human Chromatin Remodeler CHD4 (494-1353) experimental SAS data

Sample:	Human Chromatin Remodeler CHD4 (494-1353) monomer, 101 kDa Homo sapiens protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 13

R_g^Guinier	4.0	nm
D_max	14.5	nm

SASDAA5 – CHD4 (AH)

Human Chromatin Remodeler CHD4 (685-1233) experimental SAS data

Sample:	Human Chromatin Remodeler CHD4 (685-1233) monomer, 63 kDa Homo sapiens protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 13

R_g^Guinier	4.0	nm
D_max	14.5	nm

SASDAB5 – CHD4 (PP-CC)

Human Chromatin Remodeler CHD4 (363-682) experimental SAS data

Sample:	Human Chromatin Remodeler CHD4 (363-682) monomer, 38 kDa Homo sapiens protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 13

R_g^Guinier	3.0	nm
D_max	10.5	nm

SASDMR2 – HPMA-Based Nanoparticles with Cholesterol (1.4%)

N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with cholesterol 1.4% experimental SAS data

Sample:	N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with cholesterol 1.4% 0, 16272 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 27

Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system. Biomacromolecules 13(8):2594-604 (2012)
Filippov SK, Chytil P, Konarev PV, Dyakonova M, Papadakis C, Zhigunov A, Plestil J, Stepanek P, Etrych T, Ulbrich K, Svergun DI

R_g^Guinier	6.2	nm
D_max	22.0	nm

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