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Cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of YvoA from Bacillus subtilis

Cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of... The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli. The protein was purified by immobilized metal‐affinity chromatography and size‐exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50 Å resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of YvoA from Bacillus subtilis

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References (23)

Publisher
Wiley
Copyright
International Union of Crystallography, 2009
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309109008628
pmid
19342794
Publisher site
See Article on Publisher Site

Abstract

The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli. The protein was purified by immobilized metal‐affinity chromatography and size‐exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50 Å resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit.

Journal

Acta Crystallographica Section FWiley

Published: Apr 1, 2009

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