title: Crystallization and preliminary X-ray studies of the liganded lysine, arginine, ornithine-binding protein from Salmonella typhimurium.
abstract: The periplasmic binding protein LAO from Salmonella typhimurium, which is involved in lysine, arginine and ornithine transport, has been crystallized together with one of its ligands, arginine (LAO-Arg). Preliminary X-ray diffraction studies of LAO-Arg crystal show that it belongs to the orthorhombic space group P2(1)2(1)2(1) and has the unit cell dimensions of a = 37.65 A, b = 59.45 A, c = 115.91 A. Crystals of the LAO-Arg complex diffract beyond 2.0 A resolution.
authors.affiliation: Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
authors.forename: C H
authors.initials: CH
authors.lastname: Kang
authors.forename: S
authors.initials: S
authors.lastname: Gokcen
authors.forename: G F
authors.initials: GF
authors.lastname: Ames
mesh_terms: D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000378:metabolism*; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; C033849:lysyl-arginyl-ornithine-binding protein, bacteria