title: Crystallization and preliminary X-ray crystallographic data of a histidine-binding protein from Escherichia coli.
abstract: Histidine-binding protein, purified from periplasmic space of Escherichia coli K12, has been crystallized in a form suitable for X-ray analysis. Crystals of average size 0.3 mm x 0.15 mm x 0.15 mm have been grown by the hanging-drop method, with ammonium sulfate as precipitant. The space group if I4(1)22, with the unit cell dimensions a = b = 119.1 A; c = 151.8 A; Vm = 2.7 A3/dalton. There appear to be two protein subunits of molecular weight 25,000 each in the asymmetric unit.
authors.affiliation: Institute of Crystallography, Academy of Sciences of the USSR, Moscow.
authors.forename: S D
authors.initials: SD
authors.lastname: Trakhanov
authors.lastname: Chirgadze NYu
authors.forename: E F
authors.initials: EF
authors.lastname: Yusifov
mesh_terms: D001426:Bacterial Proteins; D002352:Carrier Proteins; D003460:Crystallization; D004926:Escherichia coli; D006639:Histidine / Q000378:metabolism*; D033902:Periplasmic Binding Proteins; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D033902:Periplasmic Binding Proteins; C018963:histidine-binding protein; D006639:Histidine