Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum.
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%.
Eckhard
Ulrich
U
Structural Biology Group, Department of Molecular Biology, University of Salzburg, 5020 Salzburg, Austria. ulrich.eckhard@sbg.ac.at
Nüss
Dorota
D
Ducka
Paulina
P
Schönauer
Esther
E
Brandstetter
Hans
H
D020134:Catalytic Domain; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D047009:Hathewaya histolytica / Q000201:enzymology*; D017364:Collagenases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization / Q000379:methods; D014961:X-Ray Diffraction
D017364:Collagenases