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Purification, crystallization and preliminary X-ray analysis of apo glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from methicillin-resistant Staphylococcus aureus (MRSA252).

ABSTRACT: 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.

SUBMITTER: Mukherjee S

PROVIDER: S-EPMC2864678 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray analysis of apo glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from methicillin-resistant Staphylococcus aureus (MRSA252).

Mukherjee Somnath S Saha Baisakhee B Dutta Debajyoti D Das Amit Kumar AK

Acta crystallographica. Section F, Structural biology and crystallization communications 20100429 Pt 5

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 asymmetr ...[more]

PMID: 20445245

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