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Expression, purification, crystallization and preliminary X-ray diffraction studies of triosephosphate isomerase from methicillin-resistant Staphylococcus aureus (MRSA252).

ABSTRACT: Triosephosphate isomerase 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 from 1.6 M trisodium citrate dihydrate pH 6.5 using the hanging-drop vapour-diffusion method. The crystals belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 79.15, c = 174.27 A. X-ray diffraction data were collected and processed to a maximum resolution of 1.9 A. The presence of two molecules in the asymmetric unit gave a Matthews coefficient (V(M)) of 2.64 A(3) Da(-1), with a solvent content of 53.63%.

SUBMITTER: Mukherjee S

PROVIDER: S-EPMC2664771 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray diffraction studies of triosephosphate isomerase from methicillin-resistant Staphylococcus aureus (MRSA252).

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

Acta crystallographica. Section F, Structural biology and crystallization communications 20090325 Pt 4

Triosephosphate isomerase 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 from 1.6 M trisodium citrate dihydrate pH 6.5 using the hanging-drop vapour-diffusion method. The crystals belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 79.15, c = 174.27 A. X-ray diffraction data were collected and processed to a maximum resolution of ...[more]

PMID: 19342791

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