Crystallization and preliminary X-ray analysis of methylthioribose-1-phosphate isomerase from Bacillus subtilis.
Methylthioribose-1-phosphate isomerase (MtnA) from Bacillus subtilis, the first enzyme in the downstream section of the methionine-salvage pathway, was crystallized using the sitting-drop vapour-diffusion method. Crystals grew using ammonium sulfate as the precipitant at 293 K. They diffracted to 2.5 A at 100 K using synchrotron radiation and were found to belong to the tetragonal space group P4(1), with unit-cell parameters a = b = 69.2, c = 154.7 A. The asymmetric unit contains two molecules of MtnA, with a VM value of 2.4 A3 Da(-1) and a solvent content of 48%.
Tamura
Haruka
H
Department of Materials Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan.
Matsumura
Hiroyoshi
H
Inoue
Tsuyoshi
T
Ashida
Hiroki
H
Saito
Yohtaro
Y
Yokota
Akiho
A
Kai
Yasushi
Y
D019747:Aldose-Ketose Isomerases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D000645:Ammonium Sulfate; D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D011232:Chemical Precipitation; D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D014835:Volatilization; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D019747:Aldose-Ketose Isomerases; D000645:Ammonium Sulfate