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Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis.

ABSTRACT: Crystallization and preliminary crystallographic analysis of the phosphoglucose isomerase from a Bacillus subtilis native strain were carried out. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 145.7, b = 136.0, c = 109.1 A, beta = 119.4 degrees . The diffraction quality of the crystal was significantly improved from 2.4 A to greater than 1.9 A resolution by using the in situ flash-annealing method. A 98% complete data set with an overall R(merge) of 4.6% was collected using an R-AXIS IV(++) image-plate system and a copper rotating-anode X-ray generator. The crystals contained four molecules per asymmetric unit and the predicted solvent content and the Matthews coefficient (V(M)) were 46.8% and 2.3 A(3) Da(-1), respectively. Structure determination by the molecular-replacement method provided a reasonable solution for model building.

SUBMITTER: Lee YL

PROVIDER: S-EPMC2593699 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis.

Lee Yian Liang YL Li TienHsiung Thomas TT

Acta crystallographica. Section F, Structural biology and crystallization communications 20081128 Pt 12

Crystallization and preliminary crystallographic analysis of the phosphoglucose isomerase from a Bacillus subtilis native strain were carried out. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 145.7, b = 136.0, c = 109.1 A, beta = 119.4 degrees . The diffraction quality of the crystal was significantly improved from 2.4 A to greater than 1.9 A resolution by using the in situ flash-annealing method. A 98% complete data set with an overall R(merge) of 4.6% w ...[more]

PMID: 19052382

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