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

Journal Article · Thu May 01 04:00:00 EDT 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309108010476· OSTI ID:22360570

Eckhard, Ulrich; Nüss, Dorota; Ducka, Paulina; Schönauer, Esther; Brandstetter, Hans ^[1]

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1. Structural Biology Group, Department of Molecular Biology, University of Salzburg, 5020 Salzburg (Austria)

The catalytic domain of collagenase G from C. histolyticum was expressed in E. coli BL21 (DE3) and purified using affinity and size-exclusion column-chromatographic methods. Crystals were obtained at 290 K by the sitting-drop vapour-diffusion method and diffraction data have been collected to 2.75 Å resolution. 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%.

• OSTI ID: 22360570
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 5 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AFFINITY
CITRATES
CRYSTALLIZATION
CRYSTALS
DIFFRACTION
DIFFUSION
ESCHERICHIA COLI
MOLECULES
RESOLUTION
SODIUM COMPOUNDS
SOLVENTS
SPACE GROUPS
SYNCHROTRON RADIATION