Preliminary crystallographic analysis of glutamine-binding protein from Escherichia coli.
Glutamine-binding protein from Escherichia coli, an essential component in the active transport of L-glutamine across the cytoplasmic membrane, has been crystallized by vapor diffusion in the presence of ammonium sulfate. The crystals exhibit pseudo-tetragonal symmetry with cell constants a = 77.5 A, b = 78.5 A and c = 90.2 A. Analysis of the diffraction data indicates that the space group is P2(1)2(1)2(1). There are two molecules per asymmetric unit and the solvent content is estimated to be 53%.
Chen
P
P
Department of Crystallography, University of Pittsburgh, PA 15260.
Rose
J
J
Chung
Y J
YJ
Wang
B C
BC
Shen
Q C
QC
Cottam
P F
PF
Ho
C
C
D002352:Carrier Proteins; D004926:Escherichia coli; D005973:Glutamine / Q000378:metabolism*; D014961:X-Ray Diffraction
D002352:Carrier Proteins; C037853:glutamine transport proteins; D005973:Glutamine