Crystallization and preliminary X-ray analysis of the periplasmic dipeptide binding protein from Escherichia coli.
The periplasmic dipeptide-binding protein from Escherichia coli has been purified, freed of bound endogenous ligands, and crystallized. Crystals of the protein in complex with added dipeptides have been subjected to X-ray analysis. The crystals grow as hexagonal bipyramids or eye-shaped disks which have the symmetry of space group P6(1). The unit cell dimensions are a = b = 183 A, c = 212 A, and the diffraction pattern extends to 3.2 A resolution with a conventional X-ray source.
Dunten
P W
PW
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
Harris
J H
JH
Feiz
V
V
Mowbray
S L
SL
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002352:Carrier Proteins; D003460:Crystallization; D004151:Dipeptides / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D033902:Periplasmic Binding Proteins; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D002352:Carrier Proteins; D004151:Dipeptides; D029968:Escherichia coli Proteins; D033902:Periplasmic Binding Proteins; C066768:dppA protein, E coli