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. 1999 Aug;55(Pt 8):1484-6.
doi: 10.1107/s0907444999007386.

Crystallization and X-ray crystallographic analysis of m-calpain, a Ca2+-dependent protease

C M Hosfield  1 , Q Ye, J S Arthur, C Hegadorn, D E Croall, J S Elce, Z Jia
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Crystallization and X-ray crystallographic analysis of m-calpain, a Ca2+-dependent protease

C M Hosfield et al. Acta Crystallogr D Biol Crystallogr. 1999 Aug.

Abstract

The absolute requirement of Ca(2+) for proteolytic activity is a feature unique to the calpains, a family of heterodimeric cysteine proteases. Conditions are described which give rise to diffraction-quality crystals of m-calpain in two crystal forms, P1 and P2(1). Data have been collected from native crystals of m-calpain in both P1 and P2(1) forms, to 2.6 and 2.15 A, respectively. Selenomethionine-containing crystals have been grown in both forms, and anomalous data from the P2(1) selenomethionine enzyme provided the location of 17 of the 19 Se atoms in the protein.

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