Open AccessCrystallization and preliminary X‐ray diffraction studies of the precursor protein of a thermostable variant of papain
Author(s) -
Roy Sumana,
Choudhury Debi,
Chakrabarti Chandana,
Biswas Sampa,
Dattagupta J. K.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111010888
Subject(s) - papain , crystallization , resolution (logic) , crystallography , escherichia coli , diffraction , solvent , x ray crystallography , recombinant dna , synchrotron radiation , molecule , protein crystallization , chemistry , enzyme , materials science , biochemistry , organic chemistry , physics , optics , computer science , gene , artificial intelligence
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 P 2 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.