Open AccessPurification, crystallization and preliminary X‐ray analysis of apo glyceraldehyde‐3‐phosphate dehydrogenase 1 (GAP1) from methicillin‐resistant Staphylococcus aureus (MRSA252)
Author(s) -
Mukherjee Somnath,
Saha Baisakhee,
Dutta Debajyoti,
Das Amit Kumar
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110007980
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , crystallization , staphylococcus aureus , dehydrogenase , microbiology and biotechnology , chemistry , biochemistry , biology , bacteria , enzyme , organic chemistry , genetics
Glyceraldehyde‐3‐phosphate dehydrogenase 1 (GAP1) from methicillin‐resistant Staphylococcus aureus (MRSA252) has been purified to homogeneity in the apo form. 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 = 69.95, b = 93.68, c = 89.05 Å, β = 106.84°. X‐ray diffraction data have been collected and processed to a maximum resolution of 2.2 Å. The presence of one tetramer in the asymmetric unit gives a Matthews coefficient ( V M ) of 1.81 Å 3 Da −1 with a solvent content of 32%. The structure has been solved by molecular replacement and structure refinement is now in progress.