Small Angle Scattering Biological Data Bank SASBDB

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SASDBD3 – Leishmania braziliensis heat shock protein 90 (Hsp90).

Leishmania braziliensis heat shock protein 90 (Hsp90) experimental SAS data

Sample:	Leishmania braziliensis heat shock protein 90 (Hsp90) dimer, 166 kDa Leishmania braziliensis protein
Buffer:	25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1

Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. Int J Biol Macromol 97:503-512 (2017)
Seraphim TV, Silva KP, Dores-Silva PR, Barbosa LR, Borges JC

R_g^Guinier	5.3	nm
D_max	21.0	nm
Volume^Porod	380	nm³

SASDBE3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N domain.

Leishmania braziliensis heat shock protein 90 (Hsp90) N domain experimental SAS data

Sample:	Leishmania braziliensis heat shock protein 90 (Hsp90) N domain monomer, 26 kDa Leishmania braziliensis protein
Buffer:	25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1

R_g^Guinier	2.0	nm
D_max	7.5	nm
Volume^Porod	40	nm³

SASDBF3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains.

Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains experimental SAS data

Sample:	Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains monomer, 62 kDa Leishmania braziliensis protein
Buffer:	25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1

R_g^Guinier	3.2	nm
D_max	13.0	nm
Volume^Porod	89	nm³

SASDBF7 – Dps2, DNA binding protein under starvation conditions (SEC-SAXS)

N-terminal truncated DNA protection during starvation protein 2 experimental SAS data

Sample:	N-terminal truncated DNA protection during starvation protein 2 dodecamer, 279 kDa Deinococcus radiodurans R1 protein
Buffer:	20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2013 Nov 22

SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV

R_g^Guinier	4.2	nm
D_max	12.7	nm
Volume^Porod	445	nm³

SASDBG7 – Dps1, DNA binding protein under starvation conditions (SEC-SAXS)

DNA protection during starvation protein 1 experimental SAS data

Sample:	DNA protection during starvation protein 1 dodecamer, 276 kDa Deinococcus radiodurans R1 protein
Buffer:	20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2013 Nov 22

R_g^Guinier	4.2	nm
D_max	12.8	nm
Volume^Porod	437	nm³

SASDBH7 – Dps1 truncated, DNA binding protein under starvation conditions (SEC-SAXS)

N-terminal truncated DNA protection during starvation protein 1 experimental SAS data

Sample:	N-terminal truncated DNA protection during starvation protein 1 dodecamer, 216 kDa Deinococcus radiodurans R1 protein
Buffer:	20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2013 Nov 22

R_g^Guinier	3.9	nm
D_max	10.0	nm
Volume^Porod	291	nm³

SASDDH7 – Citrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA in the presence of citrate

citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA experimental SAS data

Sample:	Citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA dimer, 77 kDa protein
Buffer:	10 mM glycine buffer, 10 mM NaCl, 1 mM sodium citrate, pH: 10
Experiment:	SAXS data collected at BM29, ESRF on 2014 Feb 6

A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase. Sci Rep 7:42592 (2017)
Kaschner M, Schillinger O, Fettweiss T, Nutschel C, Krause F, Fulton A, Strodel B, Stadler A, Jaeger KE, Krauss U

R_g^Guinier	3.3	nm
D_max	11.7	nm

SASDDJ7 – Citrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA

Sample:	Citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA dimer, 77 kDa protein
Buffer:	10 mM glycine buffer, 10 mM NaCl, pH: 10
Experiment:	SAXS data collected at BM29, ESRF on 2014 Feb 6

R_g^Guinier	3.3	nm
D_max	11.8	nm

SASDAY8 – Human alphacoronavirus non-structural protein Nsp10 in the presence of Zn

HCoV-229E Non-structural protein 10 experimental SAS data

Sample:	HCoV-229E Non-structural protein 10 monomer, 15 kDa Human coronavirus 229E protein
Buffer:	25 mM HEPES 280 mM NaCl 2 mM DTT 500 µM ZnCl2, pH: 7.6
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 25

Human alphacoronavirus non-structural protein Nsp10
Sven Falke, Al Kikhney

R_g^Guinier	1.7	nm
D_max	5.8	nm

SASDA39 – HCoV-229E Nsp10 in the absence of Zn

Sample:	HCoV-229E Non-structural protein 10 monomer, 15 kDa Human coronavirus 229E protein
Buffer:	25 mM HEPES 400 mM NaCl 1 mM EDTA 5% glycerol 40 mM NaH2PO4, pH: 7.9
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2011 Sep 8

Human alphacoronavirus non-structural protein Nsp10
Sven Falke, Al Kikhney

R_g^Guinier	1.9	nm
D_max	6.9	nm

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