## Abstract Thermitase is a thermostable member of the subtilisin family of serine proteases. Four independently determined crystal structures of the enzyme are compared in this study: a high resolution native one and three medium resolution complexes of thermitase with eglin‐c, grown from three di
Three-dimensional structure of α-chymotrypsin-eglin c complex: a crystallographic study
✍ Scribed by M. Bolognesi
- Book ID
- 103637854
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 118 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0263-7855
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📜 SIMILAR VOLUMES
## Abstract The crystal structure of the molecular complex formed by bovine α‐chymotrypsin and the recombinant serine proteinase inhibitor eglin __c__ from __Hirudo medicinalis__ has been solved using monoclinic crystals of the complex, reported previously. Four circle diffractometer data at 3.0 Å
D , = 1.39; space group Pi-(assumed from racemic nature of synthetic product). c) Crystallized from methanolethyl acetate solution: monoclinic, a = 9.94, b = 21.12, c = 14.9 A, = 92"55', V = 3039 A3, D , = 1.32 (assuming 2 = 4), D , = 1.35; space group PZJn (2nd setting). d ) Crystallized from metha