Small Angle Scattering Biological Data Bank SASBDB

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

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	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

SASDM87 – Mouse ProNGF - pro-form of the NGF (nerve growth factor)

Mouse ProNGF - pro-form of the NGF (nerve growth factor) experimental SAS data

Sample:	Mouse ProNGF - pro-form of the NGF (nerve growth factor) dimer, 100 kDa Mus musculus protein
Buffer:	50 mM Na-phosphate, pH: 7
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jul 18

Structural and functional properties of mouse proNGF. Biochem Soc Trans 34(Pt 4):605-6 (2006)
Paoletti F, Konarev PV, Covaceuszach S, Schwarz E, Cattaneo A, Lamba D, Svergun DI

R_g^Guinier	3.0	nm
D_max	11.0	nm
Volume^Porod	97	nm³

SASDAR4 – PTB full

Polypyrimidine tract-binding protein 1 experimental SAS data

Sample:	Polypyrimidine tract-binding protein 1 monomer, 57 kDa Homo sapiens protein
Buffer:	25 mM Tris 100 mM NaCl 5.0 mM DTT, pH: 7.2
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Feb 11

Conformation of polypyrimidine tract binding protein in solution. Structure 14(6):1021-7 (2006)
Petoukhov MV, Monie TP, Allain FH, Matthews S, Curry S, Svergun DI

R_g^Guinier	4.0	nm
D_max	16.5	nm

SASDN93 – Dystrophiamyotonica kinase (DMPK)

Myotonin-protein kinase experimental SAS data

Sample:	Myotonin-protein kinase monomer, 92 kDa Homo sapiens protein
Buffer:	50 mM TrisHCl 50mM NaCl, 2.5 mM-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Mar 18

Molecular insights into the self‐assembly mechanism of dystrophia myotonica kinase The FASEB Journal 20(8):1142-1151 (2006)
Garcia P, Ucurum Z, Bucher R, Svergun D, Huber T, Lustig A, Konarev P, Marino M, Mayans O

R_g^Guinier	3.9	nm
D_max	13.0	nm
Volume^Porod	173	nm³

SASDAD4 – Full length GtBP3

Sample:	full length CtBP3 tetramer, 170 kDa protein
Buffer:	25 mM Tris/HCl 250 mM NaCl, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 18

The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. Protein Sci 15(5):1042-50 (2006)
Nardini M, Svergun D, Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M

R_g^Guinier	5.1	nm
D_max	19.0	nm
Volume^Porod	330	nm³

SASDAE4 – C-terminal CtBP3

Sample:	C-term part CtBP3 dimer, 52 kDa protein
Buffer:	25 mM Tris/HCl 250 mM NaCl, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 18

R_g^Guinier	5.5	nm
D_max	20.0	nm
Volume^Porod	126	nm³

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