Open AccessCrystallization and preliminary X‐ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum
Author(s) -
Eckhard Ulrich,
Nüss Dorota,
Ducka Paulina,
Schönauer Esther,
Brandstetter Hans
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108010476
Subject(s) - orthorhombic crystal system , crystallization , chemistry , escherichia coli , crystallography , resolution (logic) , peg ratio , lysis , collagenase , catalysis , clostridium , chromatography , crystal structure , enzyme , biochemistry , bacteria , biology , organic chemistry , economics , artificial intelligence , finance , genetics , computer science , gene
The catalytic domain of collagenase G from Clostridium histolyticum has been cloned, recombinantly expressed in Escherichia coli and purified using affinity and size‐exclusion column‐chromatographic methods. Crystals of the catalytic domain were obtained from 0.12 M sodium citrate and 23%( v / v ) PEG 3350 at 293 K. The crystals diffracted to 2.75 Å resolution using synchrotron radiation. The crystals belong to an orthorhombic space group, with unit‐cell parameters a = 57, b = 109, c = 181 Å. This unit cell is consistent with the presence of one molecule per asymmetric unit and a solvent content of approximately 53%.
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