Crystallization and preliminary X-ray analysis of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from Bacillus subtilis.
2,3-Diketo-5-methylthiopentyl-1-phosphate enolase (DK-MTP-1P enolase) from Bacillus subtilis was crystallized using the hanging-drop vapour-diffusion method. Crystals grew using PEG 3350 as the precipitant at 293 K. The crystals diffracted to 2.3 A resolution at 100 K using synchrotron radiation and were found to belong to the monoclinic space group P2(1), with unit-cell parameters a = 79.3, b = 91.5, c = 107.0 A, beta = 90.8 degrees. The asymmetric unit contained four molecules of DK-MTP-1P enolase, with a V(M) value of 2.2 A(3) Da(-1) and a solvent content of 43%.
Tamura
Haruka
H
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Ashida
Hiroki
H
Koga
Shogo
S
Saito
Yohtaro
Y
Yadani
Tomonori
T
Kai
Yasushi
Y
Inoue
Tsuyoshi
T
Yokota
Akiho
A
Matsumura
Hiroyoshi
H
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010755:Organophosphates / Q000737:chemistry*; D010751:Phosphopyruvate Hydratase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D055503:Protein Multimerization; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry / Q000235:genetics
C519707:2,3-diketo-5-methylthiopentane 1-phosphate; D001426:Bacterial Proteins; D010755:Organophosphates; D011994:Recombinant Proteins; D012273:Ribulose-Bisphosphate Carboxylase; D010751:Phosphopyruvate Hydratase