Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 67, Issue -, Pages 634-636Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309111010888
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Funding
- CSIR [21/0653/06/EMR-II]
- DST [SR/WOS-A/LS-161/2004]
- DBT, Government of India
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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 angstrom, beta = 93.0 degrees, and diffracted to 2.6 angstrom resolution using synchrotron radiation. Assuming the presence of two molecules in the asymmetric unit, the calculated Matthews coefficient is 2.28 angstrom(3) Da(-1), corresponding to a solvent content of 46%. Initial attempts to solve the structure using molecular-replacement techniques were successful.
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