Abstract
X-ray quality single crystals of an extracellular esterase from pathogenic Streptomyces scabies were obtained by the hanging drop method. The crystals are monoclinic (space group C2, a = 161.1 Å, b = 51.2 Å, c = 124.2 Å, β = 100.6 °) with two molecules related by a non-crystallographic dyad in the asymmetric unit, with a solvent content of approximately 64%. The diffraction pattern from fresh crystals extends beyond 2 Å resolution using sealed tube CuKα radiation. The study has been initiated in order to elucidate the mechanism of this unusual non-serine-dependent esterase, and to gain better understanding of the molecular basis of the pathogenesis of the scab disease.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 569-571 |
| Number of pages | 3 |
| Journal | Journal of Molecular Biology |
| Volume | 227 |
| Issue number | 2 |
| DOIs | |
| State | Published - Sep 20 1992 |
Bibliographical note
Funding Information:This study is financed by the Medical Research Council of Canada grant to the Group in Protein Structure and Function (ZSD), the National Science Foundation, grant DMB-8804638 (J.L.S.), the Herman Frasch Foundat’ion. grant 0142-HF (J.L.S.) and the Agricultural Experiment Station at the IJniversity of Minnesota (J.L.S.). We thank Dr IT. Derewenda for help with computing and Koto Hayakawa for hrr help in growing crystals.
Keywords
- esterase
- hydrolase
- protein crystallization