Cloning, purification, crystallization and preliminary crystallographic analysis of Bacillus subtilis LuxS.
LuxS of Bacillus subtilis is a member of a novel family of proteins with a potential role in quorum sensing, controlling important aspects of cellular physiology in a range of microbial species. B. subtilis luxS was cloned, expressed in Escherichia coli, purified and crystallized using the hanging-drop method of vapour diffusion with ammonium sulfate as the precipitant. The crystals belong to one of the enantiomorphic space groups P6(1)22 or P6(5)22, with approximate unit-cell parameters a = b = 63.6, c = 151.5 A and one subunit in the asymmetric unit, corresponding to a packing density of 2.5 A(3) Da(-1). The crystals diffract X-rays to at least 1.55 A resolution on a synchrotron-radiation source. Determination of the structure will provide insights into the key determinants of function of this class of proteins, for which no structures are currently available.
Das
S K
SK
The Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, England.
Sedelnikova
S E
SE
Baker
P J
PJ
Ruzheinikov
S N
SN
Foster
S
S
Hartley
A
A
Horsburgh
M J
MJ
Rice
D W
DW
D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D013437:Carbon-Sulfur Lyases; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D013437:Carbon-Sulfur Lyases; C117753:LuxS protein, Bacteria