title: Preliminary crystallographic analysis of glutamine-binding protein from Escherichia coli.
abstract: 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%.
authors.affiliation: Department of Crystallography, University of Pittsburgh, PA 15260.
authors.forename: P
authors.initials: P
authors.lastname: Chen
authors.forename: J
authors.initials: J
authors.lastname: Rose
authors.forename: Y J
authors.initials: YJ
authors.lastname: Chung
authors.forename: B C
authors.initials: BC
authors.lastname: Wang
authors.forename: Q C
authors.initials: QC
authors.lastname: Shen
authors.forename: P F
authors.initials: PF
authors.lastname: Cottam
authors.forename: C
authors.initials: C
authors.lastname: Ho
mesh_terms: D002352:Carrier Proteins; D004926:Escherichia coli; D005973:Glutamine / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D002352:Carrier Proteins; C037853:glutamine transport proteins; D005973:Glutamine