Detalle de: Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum
| Title | 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%. |
| Apa Reference | Eckhard, U., Nüss, D., Ducka, P., Schönauer, E., & Brandstetter, H. (2008). Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G fromClostridium histolyticum. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 64(5), 419–421. 10.1107/s1744309108010476 |
| Doi | 10.1107/S1744309108010476 |
| Publication Date | 24 Apr 2008 |
| Publication Type | Article |
| Researcher | Ulrich Eckhard |
| Ontology | Model organisms |
| Research Groups | Synthetic Structural Biology |
| Tools |