Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 5 (May 2008)

crystallization communications

Acta Cryst. (2008). F64, 419-421 [ doi:10.1107/S1744309108010476 ]

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

U. Eckhard, D. Nüss, P. Ducka, E. Schönauer and H. Brandstetter

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 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%.

Keywords: collagenase G; Clostridium histolyticum.