Crystallization and preliminary X-ray analysis of ervatamin B and C, two thiol proteases from Ervatamia coronaria

Authors
Chakrabarti, C Biswas, S Kundu, S Sundd, M Jagannadham, MV Dattagupta, JK
Citation
C. Chakrabarti et al., Crystallization and preliminary X-ray analysis of ervatamin B and C, two thiol proteases from Ervatamia coronaria, ACT CRYST D, 55, 1999, pp. 1074-1075
Citations number
10
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
55
Year of publication
1999
Part
5
Pages
1074 - 1075
Database
ISI
SICI code
0907-4449(199905)55:<1074:CAPXAO>2.0.ZU;2-A
Abstract
Two highly stable cysteine proteases, ervatamin B (ERV-B) and ervatamin C ( ERV-C), purified from the latex of the medicinal plant E. coronaria have be en crystallized at room temperature. Crystals of ERV-B and ERV-C diffract t o 2.5 and 2.6 Angstrom, respectively. The space group is P2(1)2(1)2(1) for the crystals of both proteases with unit-call parameters a = 47.5, b = 58.8 and c = 68.8 Angstrom, and a = 43.8, b = 82.6 and c = 133.1 Angstrom, resp ectively. A self-rotation function for ERV-C indicates a twofold non-crysta llographic symmetry relating the two molecules in the asymmetric unit.