Structure of the proteinase inhibitor eglin c with hydrolysed reactive centre at 2.0 Å resolution
✍ Scribed by Christian Betzel; Zbigniew Dauter; Nicolay Genov; Victor Lamzin; Jorge Navaza; Hans Peter Schnebli; Marcia Visan; Keith S. Wilson
- Book ID
- 115928319
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 429 KB
- Volume
- 317
- Category
- Article
- ISSN
- 0014-5793
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## 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
The crystal structure of the zinc-saturated C-terminal lobe of bovine lactoferrin has been determined at 2.0 A resolution using crystals stabilized at pH 3.8. This is the first metal-saturated structure of any functional lactoferrin at such a low pH. Purified samples of proteolytically generated zin