Small Angle Scattering Biological Data Bank SASBDB

Browse by DISSEMINATION: Published

SASDAN3 – MutS dimer

DNA mismatch repair protein MutS experimental SAS data

Sample:	DNA mismatch repair protein MutS dimer, 191 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Feb 28

Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK

R_g^Guinier	4.7	nm
D_max	15.5	nm
Volume^Porod	307	nm³

SASDAQ3 – MutS tetramer

Sample:	DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12

R_g^Guinier	7.8	nm
D_max	28.0	nm
Volume^Porod	700	nm³

SASDAX3 – MutS tetramer

DNA mismatch repair protein MutS Kratky plot

Sample:	DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12

R_g^Guinier	8.5	nm
D_max	29.0	nm
Volume^Porod	750	nm³

SASDAY3 – MutS tetramer

Sample:	DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12

R_g^Guinier	8.3	nm
D_max	29.0	nm
Volume^Porod	720	nm³

SASDAZ3 – MutS tetramer

Sample:	DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12

R_g^Guinier

8.0

SASDA24 – MutS tetramer

Sample:	DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12

R_g^Guinier	7.8	nm
D_max	27.0	nm

SASDA45 – PpoA wild type enzyme

Psi-producing oxygenase A experimental SAS data

Sample:	Psi-producing oxygenase A trimer, 362 kDa Aspergillus nidulans protein
Buffer:	20 Mm HEPES, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Jun 24

A structural model of PpoA derived from SAXS-analysis-implications for substrate conversion. Biochim Biophys Acta 1831(9):1449-57 (2013)
Koch C, Tria G, Fielding AJ, Brodhun F, Valerius O, Feussner K, Braus GH, Svergun DI, Bennati M, Feussner I

R_g^Guinier	5.4	nm
D_max	16.5	nm
Volume^Porod	540	nm³

SASDAJ4 – CRM1

Sample:	Exportin-1 monomer, 123 kDa Mus musculus protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3

Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A

R_g^Guinier	3.8	nm
D_max	11.0	nm
Volume^Porod	190	nm³

SASDAK4 – CRM1 RanGTP

Exportin-1GTP-binding nuclear protein Ran experimental SAS data

Sample:	Exportin-1 monomer, 123 kDa Mus musculus protein GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3

R_g^Guinier	3.6	nm
D_max	10.0	nm

SASDAL4 – CRM1 RanGTP Snu1

Exportin-1GTP-binding nuclear protein RanSnurportin-1 experimental SAS data

Sample:	Exportin-1 monomer, 123 kDa Mus musculus protein GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein Snurportin-1 monomer, 41 kDa Homo sapiens protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3

R_g^Guinier	4.1	nm
D_max	14.0	nm

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