Small Angle Scattering Biological Data Bank SASBDB

Browse by ORGANISM: Mus musculus (Mouse)

SASDAS5 – ad11 Fab

Sample:	AD11 Fab dimer, 50 kDa Mus musculus protein
Buffer:	50 mM Na-phosphate 1mM ethylenediaminetetraacetic aci, pH: 7
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 20

Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody. J Mol Biol 381(4):881-96 (2008)
Covaceuszach S, Cassetta A, Konarev PV, Gonfloni S, Rudolph R, Svergun DI, Lamba D, Cattaneo A

R_g^Guinier	2.6	nm
D_max	8.0	nm
Volume^Porod	95	nm³

SASDAT5 – NGF

Sample:	NGF dimer, 50 kDa Mus musculus protein
Buffer:	10 mM Na-phosphate 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 20

R_g^Guinier	3.1	nm
D_max	12.0	nm
Volume^Porod	102	nm³

SASDAU5 – ad11 Fab + NGF

Sample:	AD11 Fab dimer, 50 kDa Mus musculus protein NGF dimer, 50 kDa Mus musculus protein
Buffer:	30 mM Na-phosphate 75 mM NaCl, pH: 7
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Dec 20

R_g^Guinier	4.3	nm
D_max	16.0	nm
Volume^Porod	255	nm³

SASDMT4 – Complex of Met receptor with InlB

Hepatocyte growth factor receptorInternalin B experimental SAS data

Sample:	Hepatocyte growth factor receptor monomer, 100 kDa Mus musculus protein Internalin B monomer, 36 kDa Listeria monocytogenes serotype … protein
Buffer:	25mM Na-phosphate buffer, 150 mM NaCl, 1mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Mar 1

X-ray and Neutron Small-Angle Scattering Analysis of the Complex Formed by the Met Receptor and the Listeria monocytogenes Invasion Protein InlB Journal of Molecular Biology 377(2):489-500 (2008)
Niemann H, Petoukhov M, Härtlein M, Moulin M, Gherardi E, Timmins P, Heinz D, Svergun D

R_g^Guinier	4.6	nm
D_max	16.0	nm
Volume^Porod	270	nm³

SASDH43 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN)

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data

Sample:	N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer:	15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, pH: 8
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12

Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M

R_g^Guinier	3.2	nm
D_max	10.0	nm
Volume^Porod	135	nm³

SASDH53 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with calcium

Sample:	N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer:	15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, pH: 8
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12

R_g^Guinier	3.4	nm
D_max	11.0	nm
Volume^Porod	160	nm³

SASDH63 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3)

Sample:	N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer:	15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, 0.25 mM IP3, pH: 8
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12

R_g^Guinier	3.1	nm
D_max	8.8	nm
Volume^Porod	115	nm³

SASDH73 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3) plus calcium

Sample:	N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer:	15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, 0.25 mM IP3, pH: 8
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12

R_g^Guinier	3.2	nm
D_max	9.6	nm
Volume^Porod	132	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

SASDLP7 – Two-chain hepatocyte growth factor/scatter factor in complex with receptor tyrosine kinase MET

Hepatocyte growth factorHepatocyte growth factor receptor experimental SAS data

Sample:	Hepatocyte growth factor monomer, 79 kDa Mus musculus protein Hepatocyte growth factor receptor monomer, 100 kDa Mus musculus protein
Buffer:	50 mM MES, 150 mM NaCl, pH: 6.7
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Feb 9

Structural basis of hepatocyte growth factor/scatter factor and MET signalling Proceedings of the National Academy of Sciences 103(11):4046-4051 (2006)
Gherardi E, Sandin S, Petoukhov M, Finch J, Youles M, Ofverstedt L, Miguel R, Blundell T, Vande Woude G, Skoglund U, Svergun D

R_g^Guinier	6.7	nm
D_max	20.0	nm
Volume^Porod	370	nm³

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