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Purification and preliminary crystallographic studies on the sporulation response regulatory phosphotransferase protein, spo0B, from Bacillus subtilis
Author(s) -
Zhou Xiao Zhen,
Whiteley J.M.,
Hoch J.A.,
Varughese K.I.
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199704)27:4<597::aid-prot11>3.0.co;2-f
Subject(s) - bacillus subtilis , pep group translocation , phosphotransferase , escherichia coli , chemistry , strain (injury) , spore , synchrotron , crystallography , biology , biochemistry , enzyme , microbiology and biotechnology , bacteria , gene , genetics , physics , anatomy , nuclear physics
The phosphotransferase protein Spo0B, a component of the sporulation signal transduction system in Bacillus subtilis was expressed from the Escherichia coli strain BL21DE3. It was purified, crystallized, and 2.25 Å data measured using the synchrotron source at the Stanford Linear Accelerator Center. The search for heavy atom derivatives is in progress. © 1997 Wiley‐Liss Inc.