Open AccessCrystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis
Author(s) -
Lee Yian Liang,
Li TienHsiung Thomas
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108037718
Subject(s) - monoclinic crystal system , crystallization , bacillus subtilis , glucose 6 phosphate isomerase , crystallography , annealing (glass) , isomerase , crystal (programming language) , molecule , materials science , chemistry , resolution (logic) , crystal structure , biochemistry , biology , enzyme , bacteria , organic chemistry , artificial intelligence , computer science , programming language , composite material , genetics
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 C 2, with unit‐cell parameters a = 145.7, b = 136.0, c = 109.1 Å, β = 119.4°. The diffraction quality of the crystal was significantly improved from 2.4 Å to greater than 1.9 Å 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 Å 3 Da −1 , respectively. Structure determination by the molecular‐replacement method provided a reasonable solution for model building.