| Literature DB >> 8845771 |
Abstract
We have expressed active human cathepsin S to 60 mg/L in Sf9 cells using a baculovirus system. Production of milligram quantities has facilitated crystallographic studies to determine the structure of this enzyme, which has unique properties among lysosomal cysteine proteinases. Recombinant, irreversibly inhibited cathepsin S was crystallized from ammonium phosphate at 17 degrees C. The crystals diffract to at least 2.3 A, and belong to the orthorhombic crystal system with a primitive lattice. Approximate cell dimensions are: a = 37.7 A, b = 73.9 A, and c = 106.7 A. There is most likely one molecule per asymmetric unit.Entities:
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Year: 1996 PMID: 8845771 PMCID: PMC2143400 DOI: 10.1002/pro.5560050426
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725