Purification, crystallization and preliminary X-ray analysis of apo glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from methicillin-resistant Staphylococcus aureus (MRSA252).
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 P2(1), with unit-cell parameters a = 69.95, b = 93.68, c = 89.05 A, beta = 106.84 degrees . X-ray diffraction data have been collected and processed to a maximum resolution of 2.2 A. The presence of one tetramer in the asymmetric unit gives a Matthews coefficient (V(M)) of 1.81 A(3) Da(-1) with a solvent content of 32%. The structure has been solved by molecular replacement and structure refinement is now in progress.
Mukherjee
Somnath
S
Department of Biotechnology, Indian Institute of Technology, Kharagpur 721 302, India.
Saha
Baisakhee
B
Dutta
Debajyoti
D
Das
Amit Kumar
AK
D001051:Apoenzymes / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000302:isolation & purification; D055624:Methicillin-Resistant Staphylococcus aureus / Q000201:enzymology*
D001051:Apoenzymes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
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