title: Crystallization and preliminary X-ray analysis of ervatamin B and C, two thiol proteases from Ervatamia coronaria.
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 been crystallized at room temperature. Crystals of ERV-B and ERV-C diffract to 2.5 and 2.6 A, respectively. The space group is P212121 for the crystals of both proteases with unit-cell parameters a = 47.5, b = 58.8 and c = 68.8 A, and a = 43.8, b = 82.6 and c = 133.1 A, respectively. A self-rotation function for ERV-C indicates a twofold non-crystallographic symmetry relating the two molecules in the asymmetric unit.
authors.affiliation: Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF Bidhan Nagar, Calcutta 700 064, India.
authors.forename: C
authors.initials: C
authors.lastname: Chakrabarti
authors.forename: S
authors.initials: S
authors.lastname: Biswas
authors.forename: S
authors.initials: S
authors.lastname: Kundu
authors.forename: M
authors.initials: M
authors.lastname: Sundd
authors.forename: M V
authors.initials: MV
authors.lastname: Jagannadham
authors.forename: J K
authors.initials: JK
authors.lastname: Dattagupta
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D010946:Plants, Medicinal / Q000201:enzymology*; D011487:Protein Conformation
chemical_list: D010940:Plant Proteins; D003546:Cysteine Endopeptidases; C116225:ervatamin