Crystallization and preliminary X-ray studies of the liganded lysine, arginine, ornithine-binding protein from Salmonella typhimurium.
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.
Kang
C H
CH
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Gokcen
S
S
Ames
G F
GF
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
D001426:Bacterial Proteins; D002352:Carrier Proteins; C033849:lysyl-arginyl-ornithine-binding protein, bacteria