title: Crystallization of the met repressor from Escherichia coli.
abstract: The met repressor from Escherichia coli has been crystallized in space group P21, with unit cell dimensions a = 35.6 A, b = 62.6 A, c = 44.5 A, beta = 102.4 degrees and one aporepressor dimer per asymmetric unit. Preliminary X-ray diffraction photographs show measurable intensities to beyond 1.5 A resolution, and the crystal form is ideally suited to high-resolution crystallographic analysis (1 A = 0.1 nm).
authors.affiliation: Astbury Department of Biophysics, University of Leeds, U.K.
authors.forename: J B
authors.initials: JB
authors.lastname: Rafferty
authors.forename: S E
authors.initials: SE
authors.lastname: Phillips
authors.forename: C
authors.initials: C
authors.lastname: Rojas
authors.forename: G
authors.initials: G
authors.lastname: Boulot
authors.forename: I
authors.initials: I
authors.lastname: Saint-Girons
authors.forename: Y
authors.initials: Y
authors.lastname: Guillou
authors.forename: G N
authors.initials: GN
authors.lastname: Cohen
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics*; D008715:Methionine / Q000235:genetics*; D012097:Repressor Proteins; D014157:Transcription Factors
chemical_list: D001426:Bacterial Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D008715:Methionine