Small Angle Scattering Biological Data Bank SASBDB

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

SASDAC4 – FilaminC 23-24

Sample:	Filamin C 23-24 dimer, 40 kDa Escherichia coli protein
Buffer:	20 mM Tris-HCl 50 mM NaCl, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III on 2005 Jun 17

Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. J Mol Biol 368(4):1011-23 (2007)
Sjekloća L, Pudas R, Sjöblom B, Konarev P, Carugo O, Rybin V, Kiema TR, Svergun D, Ylänne J, Djinović Carugo K

R_g^Guinier	3.5	nm
D_max	13.0	nm
Volume^Porod	75	nm³

SASDHY3 – KinA-Sda complex

Sporulation kinase ASporulation inhibitor sda experimental SAS data

Sample:	Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein Sporulation inhibitor sda dimer, 11 kDa Bacillus subtilis protein
Buffer:	50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Nov 16

The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368(2):407-20 (2007)
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB

R_g^Guinier	2.9	nm
D_max	8.0	nm
Volume^Porod	85	nm³

SASDHZ3 – Sporulation kinase A

Sporulation kinase A experimental SAS data

Sample:	Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein
Buffer:	50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Mar 18

R_g^Guinier	2.9	nm
D_max	9.5	nm
Volume^Porod	76	nm³

SASDA68 – Aldolase in Tris/HCl

Fructose-bisphosphate aldolase A experimental SAS data

Sample:	Fructose-bisphosphate aldolase A tetramer, 157 kDa Oryctolagus cuniculus protein
Buffer:	100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III 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	3.6	nm
D_max	10.5	nm

SASDA78 – Carbonic Anhydrase in Tris/HCl

Carbonic anhydrase 2 experimental SAS data

Sample:	Carbonic anhydrase 2 monomer, 29 kDa Bos taurus protein
Buffer:	100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III 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	2.1	nm
D_max	6.0	nm

SASDA98 – Thyroglobulin in Tris/HCl

Sample:	Thyroglobulin dimer, 606 kDa Bos taurus protein
Buffer:	100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III 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	7.9	nm
D_max	24.0	nm

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