Crystals of glutamine-binding protein in various conformational states.
Crystals of glutamine-binding protein (GlnBP) in various conformational states have been obtained. Crystals of the ligand-free "open" state (denoted form B) have unit cell dimensions a = 86.3 A, b = 86.3 A, c = 81.5 A, alpha = beta = gamma = 90 degrees and diffract to about 2.3 A resolution. An analysis of the intensity data using an Requiv plot indicates that the crystal system is orthorhombic, space group P2(1)2(1)2(1). Crystals of the ligand-bound "open" state (form B*) are obtained by soaking form B crystals with glutamine (Gln) and diffract to about 1.9 A. Crystals of the GlnBP-Gln complex in a ligand-bound "closed" state (form C) belong to space group P2(1)2(1)2(1) with a = 62.0 A, b = 65.7 A and c = 121.8 A and diffract to about 2.3 A. Crystals of a selenomethionyl GlnBP (form B') are isomorphous to form B crystals and diffract to about 2.1 A resolution.
Hsiao
C D
CD
Department of Crystallography, University of Pittsburgh, PA 15260.
Sun
Y J
YJ
Rose
J
J
Cottam
P F
PF
Ho
C
C
Wang
B C
BC
D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000378:metabolism; D005973:Glutamine / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D011487:Protein Conformation; D012645:Selenomethionine / Q000378:metabolism
D002352:Carrier Proteins; D008024:Ligands; C037853:glutamine transport proteins; D005973:Glutamine; D012645:Selenomethionine