Expression, purification, crystallization and preliminary X-ray studies of Vibrio cholerae pseudopilin EpsH.
EpsH is a minor pseudopilin protein of the Vibrio cholerae type II secretion system. A truncated form of EpsH with a C-terminal noncleavable His tag was constructed and expressed in Escherichia coli, purified and crystallized by sitting-drop vapor diffusion. A complete data set was collected to 1.71 A resolution. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.39, b = 71.11, c = 84.64 A. There were two protein molecules in the asymmetric unit, which gave a Matthews coefficient V(M) of 2.1 A(3) Da(-1), corresponding to 41.5% solvent content.
Raghunathan
Kannan
K
Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA.
Vago
Frank S
FS
Ball
Terry
T
Yakubova
Nafissa
N
Grindem
David
D
Wedemeyer
William J
WJ
Arvidson
Dennis N
DN
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D014734:Vibrio cholerae / Q000737:chemistry*
D001426:Bacterial Proteins