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Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum.

ABSTRACT: 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 A resolution using synchrotron radiation. The crystals belong to an orthorhombic space group, with unit-cell parameters a = 57, b = 109, c = 181 A. This unit cell is consistent with the presence of one molecule per asymmetric unit and a solvent content of approximately 53%.

SUBMITTER: Eckhard U

PROVIDER: S-EPMC2376405 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum.

Eckhard Ulrich U Nüss Dorota D Ducka Paulina P Schönauer Esther E Brandstetter Hans H

Acta crystallographica. Section F, Structural biology and crystallization communications 20080424 Pt 5

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 A resolution using synchrotron radiation. The crystals belong to an orthorhombic space group, with unit-cell parameters a = 57, b = 109, c = 181 A. This u ...[more]

PMID: 18453715

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