Unknown

Dataset Information

0

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

Json Xml
altmetric image

Publications

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]

Similar Datasets

Unknown Ca2+-induced linker transformation leads to a compact and rigid collagen-binding domain of Clostridium histolyticum collagenase.
| S-EPMC2782454 | biostudies-literature
Unknown Safety and tolerability of collagenase Clostridium histolyticum and fasciectomy for Dupuytren's contracture.
| S-EPMC4361465 | biostudies-literature
Unknown Monitoring the Degradation of Collagen Hydrogels by Collagenase <i>Clostridium histolyticum</i>.
| S-EPMC7709630 | biostudies-literature
Unknown Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase.
| S-EPMC3310545 | biostudies-literature
Unknown Purification, crystallization and preliminary X-ray characterization of the pentamodular arabinoxylanase CtXyl5A from Clostridium thermocellum.
| S-EPMC3144809 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina.
| S-EPMC2374253 | biostudies-literature
Unknown Collagenase Clostridium Histolyticum for the Treatment of Edematous Fibrosclerotic Panniculopathy (Cellulite): A Randomized Trial.
| S-EPMC6693937 | biostudies-literature
Unknown Efficacy, Safety, and Durability of Response of Collagenase Clostridium Histolyticum-aaes for Treating Cellulite.
| S-EPMC7787338 | biostudies-literature
Unknown Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of membrane type 1 matrix metalloproteinase.
| S-EPMC3936455 | biostudies-literature
Unknown Protein expression, characterization, crystallization and preliminary X-ray crystallographic analysis of a Fic protein from Clostridium difficile.
| S-EPMC4051547 | biostudies-literature