title: 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, 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(-1), corresponding to a solvent content of 46%. Initial attempts to solve the structure using molecular-replacement techniques were successful.
authors.affiliation: Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700 064, India.
authors.forename: Sumana
authors.initials: S
authors.lastname: Roy
authors.forename: Debi
authors.initials: D
authors.lastname: Choudhury
authors.forename: Chandana
authors.initials: C
authors.lastname: Chakrabarti
authors.forename: Sampa
authors.initials: S
authors.lastname: Biswas
authors.forename: J K
authors.initials: JK
authors.lastname: Dattagupta
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D008969:Molecular Sequence Data; D010206:Papain / Q000737:chemistry*; D011498:Protein Precursors / Q000737:chemistry*; D013696:Temperature
chemical_list: D011498:Protein Precursors; D010206:Papain