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Crystallization and preliminary X-ray diffraction studies of the precursor protein of a thermostable variant of papain.

ABSTRACT: The crystallization of a recombinant thermostable variant of pro-papain has been carried out. The mutant pro-enzyme was expressed in Escherichia coli as inclusion bodies, refolded, purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 42.9, b = 74.8, c = 116.5 Å, ? = 93.0°, and diffracted to 2.6 Å resolution using synchrotron radiation. Assuming the presence of two molecules in the asymmetric unit, the calculated Matthews coefficient is 2.28 Å(3) Da(-1), corresponding to a solvent content of 46%. Initial attempts to solve the structure using molecular-replacement techniques were successful.

SUBMITTER: Roy S

PROVIDER: S-EPMC3087658 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction studies of the precursor protein of a thermostable variant of papain.

Roy Sumana S Choudhury Debi D Chakrabarti Chandana C Biswas Sampa S Dattagupta J K JK

Acta crystallographica. Section F, Structural biology and crystallization communications 20110428 Pt 5

The crystallization of a recombinant thermostable variant of pro-papain has been carried out. The mutant pro-enzyme was expressed in Escherichia coli as inclusion bodies, refolded, purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 42.9, b = 74.8, c = 116.5 Å, β = 93.0°, and diffracted to 2.6 Å resolution using synchrotron radiation. Assuming the presence of two molecules in the asymmetric unit, the calculated Matthews coefficient is 2.28 Å(3) Da ...[more]

PMID: 21543879

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