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Crystallization and preliminary x-ray diffraction studies of human procathepsin L

✍ Scribed by René Coulombe; Yunge Li; Sachiko Takebe; Robert Ménard; Patrizia Mason; John S. Mort; Miroslaw Cygler

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
280 KB
Volume
25
Category
Article
ISSN
0887-3585

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✦ Synopsis

Human procathepsin L has been expressed in the yeast Pichiapastoris and its inactive (Cys25Ser) and unglycosylated (ThrllOAla) mutant purified, concentrated to 4 mglml, and crystallized by vapor diffusion against solution containing 1.4 M (Na,K)PO, buffer, pH 7.8. Crystal size was increased by multiple macroseeding. The crystals are orthorhombic, of space group P2,2,2,, with cell dimensions of a = 40.2 A, b = 88.4 A, and c = 94.9 A. A 2.2 A native data set was collected using synchrotron radiation. Although molecular replacement solution for the mature portion of the enzyme was easily found, the resulting maps could not be interpreted in the proregion. Heavy-atom derivative search is in progress.

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