High level expression and crystallization of recombinant human cathepsin S.
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.
Brömme
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Khepri Pharmaceuticals, Inc., South San Francisco, California 94080, USA.
McGrath
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D016367:Baculoviridae; D002403:Cathepsins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D006801:Humans; D008297:Male; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D013737:Testis / Q000201:enzymology
D011994:Recombinant Proteins; D002403:Cathepsins; C028217:cathepsin S