Open AccessExpression, purification, crystallization and preliminary X‐ray diffraction studies of glyceraldehyde‐3‐phosphate dehydrogenase 1 from methicillin‐resistant Staphylococcus aureus (MRSA252)
Author(s) -
Mukherjee Somnath,
Dutta Debajyoti,
Saha Baisakhee,
Das Amit Kumar
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108027504
Subject(s) - tetramer , dehydrogenase , escherichia coli , crystallization , staphylococcus aureus , glyceraldehyde 3 phosphate dehydrogenase , crystallography , x ray crystallography , chemistry , diffraction , microbiology and biotechnology , materials science , biology , bacteria , biochemistry , enzyme , physics , gene , optics , genetics , organic chemistry
Glyceraldehyde‐3‐phosphate dehydrogenase 1 from methicillin‐resistant Staphylococcus aureus (MRSA252) was cloned in pQE30 vector, overexpressed in Escherichia coli M15(pREP4) cells and purified to homogeneity. The protein was crystallized using the hanging‐drop vapour‐diffusion method. The crystals belonged to space group P 2 1 , with unit‐cell parameters a = 65.23, b = 95.58, c = 87.91 Å, β = 106.5°. X‐ray diffraction data were collected and processed to a maximum resolution of 2.0 Å. The presence of one tetramer in the asymmetric unit gave a Matthews coefficient ( V M ) of 1.78 Å 3 Da −1 and a solvent content of 31%. The structure was solved by molecular replacement and structure refinement is now in progress.