FEBS Letters | |
Crystal structure of a complex between thermitase from Thermoactinomyces vulgaris and the leech inhibitor eglin | |
Dauter, Zbigniew1  Betzel, Christian1  Wilson, Keith S.1  Höhne, Wolfgang-Ernst2  Ingelman, Margareta1  | |
[1] European Molecular Biology Laboratory, c/o DESY, Notkestrasse 85, D-2000 Hamburg 52, FRG;Institut für Biochemie, Humboldt-Universität Berlin, Hessische Strasse 3-4, DDR-1040 Berlin, GDR | |
关键词: Thermitase; Serine proteinase; Crystallography; Thermostability; Molecular replacement; Ca2+ binding; | |
DOI : 10.1016/0014-5793(88)80309-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Thermitase, the thermostable alkaline protease from Thermoactinomyces vulgaris, has been crystallised in a 1:1 complex with eglin, the inhibitor from the medical leech. Two large crystals were grown, with cell dimensions of a = 49.3 Å, b = 67.3 Å, c = 90.5 Å and space group P212121. The crystals are relatively tightly packed with V m = 2.1 Å3/Da. Three-dimensional data to 1.9 Å have been recorded from one of these crystals. The orientation and position of the complex in the unit cell have been established using the subtilisin Carlsberg-eglin structure as a model. The structure of the complex is being refined by restrained least-squares. The present crystallographic R factor (= Σ|F o−F c|/Σ|F o) is 26% at 2.5 Å resolution.
【 授权许可】
Unknown
【 预 览 】
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