Small Angle Scattering Biological Data Bank SASBDB

SASDAA8 – Chymotrypsinogen A in Tris/HCl

Chymotrypsinogen A experimental SAS data

Sample:	Chymotrypsinogen A monomer, 26 kDa Bos taurus protein
Buffer:	100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 19

Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering Journal of Applied Crystallography 40(s1):s245-s249 (2007)
Mylonas E, Svergun D

R_g^Guinier	1.9	nm
D_max	5.0	nm

SASDMA7 – Prion protein aggregate in solution

Major prion protein experimental SAS data

Sample:	Major prion protein 24-mer, 664 kDa Homo sapiens protein
Buffer:	5 mM sodium acetate, pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jun 2

Structural characterization of beta-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro. J Struct Biol 157(2):308-20 (2007)
Redecke L, von Bergen M, Clos J, Konarev PV, Svergun DI, Fittschen UE, Broekaert JA, Bruns O, Georgieva D, Mandelkow E, Genov N, Betzel C

R_g^Guinier	9.8	nm
D_max	32.0	nm
Volume^Porod	3320	nm³

SASDNB2 – Human NK inhibitory receptor IRp60 with an immunoglobulin-like fold

CMRF35-like molecule 8 experimental SAS data

Sample:	CMRF35-like molecule 8 monomer, 12 kDa Homo sapiens protein
Buffer:	MES buffer with 3mM DTT, pH: 5.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Apr 6

Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a) International Journal of Biological Macromolecules 40(3):193-200 (2007)
Dimasi N, Roessle M, Moran O, Candiano G, Svergun D, Biassoni R

R_g^Guinier	2.0	nm
D_max	7.0	nm
Volume^Porod	22	nm³

SASDLR7 – The HC Fragment of Tetanus Toxin

Hc fragment of Tetanus toxin experimental SAS data

Sample:	Hc fragment of Tetanus toxin dimer, 103 kDa Clostridium tetani (strain … protein
Buffer:	50 mM sodium phosphate buffer, 300 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 May 14

The HC fragment of tetanus toxin forms stable, concentration-dependent dimers via an intermolecular disulphide bond. J Mol Biol 365(1):123-34 (2007)
Qazi O, Bolgiano B, Crane D, Svergun DI, Konarev PV, Yao ZP, Robinson CV, Brown KA, Fairweather N

R_g^Guinier	4.0	nm
D_max	13.2	nm
Volume^Porod	150	nm³

SASDN92 – Apoform of glyceraldehyde-3-phosphate dehydrogenase (apo-kmGAPDH1p)

Glyceraldehyde-3-phosphate dehydrogenase 1 experimental SAS data

Sample:	Glyceraldehyde-3-phosphate dehydrogenase 1 tetramer, 142 kDa Kluyveromyces marxianus protein
Buffer:	150 mM NaCl, 1 mM beta-mercaptoethanol, 1 mM EDTA, 10 mM TrisHCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Mar 27

The Crystal and Solution Structures of Glyceraldehyde-3-phosphate Dehydrogenase Reveal Different Quaternary Structures Journal of Biological Chemistry 281(44):33433-33440 (2006)
Ferreira-da-Silva F, Pereira P, Gales L, Roessle M, Svergun D, Moradas-Ferreira P, Damas A

R_g^Guinier	4.2	nm
D_max	12.0	nm
Volume^Porod	234	nm³

SASDNA2 – Glyceraldehyde-3-phosphate dehydrogenase (apo-kmGAPDH1p) upon NAD+ binding

Glyceraldehyde-3-phosphate dehydrogenase 1 bound to NAD+ experimental SAS data

Sample:	Glyceraldehyde-3-phosphate dehydrogenase 1 bound to NAD+ tetramer, 142 kDa Kluyveromyces marxianus protein
Buffer:	150 mM NaCl, 1 mM beta-mercaptoethanol, 1 mM EDTA, 10 mM TrisHCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Mar 27

R_g^Guinier	3.7	nm
D_max	9.9	nm
Volume^Porod	202	nm³

SASDAQ5 – Lumazine Synthase

Sample:	Lumazine Synthase , 960 kDa Bacillus subtilis protein
Buffer:	Borate buffer, pH: 7
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 25

Multiple assembly states of lumazine synthase: a model relating catalytic function and molecular assembly. J Mol Biol 362(4):753-70 (2006)
Zhang X, Konarev PV, Petoukhov MV, Svergun DI, Xing L, Cheng RH, Haase I, Fischer M, Bacher A, Ladenstein R, Meining W

R_g^Guinier	6.2	nm
D_max	15.5	nm
Volume^Porod	1450	nm³

SASDN63 – Microtubule affinity regulating kinase (isoform MARK2, T208E point mutant)

Serine/threonine-protein kinase MARK2 experimental SAS data

Sample:	Serine/threonine-protein kinase MARK2 monomer, 36 kDa Homo sapiens protein
Buffer:	0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 16

Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2 Journal of Biological Chemistry 281(37):27586-27599 (2006)
Marx A, Nugoor C, Müller J, Panneerselvam S, Timm T, Bilang M, Mylonas E, Svergun D, Mandelkow E, Mandelkow E

R_g^Guinier	2.4	nm
D_max	8.0	nm
Volume^Porod	61	nm³

SASDN73 – Microtubule affinity regulating kinase (isoform MARK2, wild type)

Sample:	Serine/threonine-protein kinase MARK2 monomer, 36 kDa Homo sapiens protein
Buffer:	0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 16

R_g^Guinier	2.3	nm
D_max	8.0	nm
Volume^Porod	62	nm³

SASDN83 – Microtubule affinity regulating kinase (isoform MARK1)

Serine/threonine-protein kinase MARK1 experimental SAS data

Sample:	Serine/threonine-protein kinase MARK1 monomer, 37 kDa Homo sapiens protein
Buffer:	0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 16

R_g^Guinier	2.3	nm
D_max	8.0	nm
Volume^Porod	64	nm³

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