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

The absolute requirement of Ca2+ 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 P21. Data have been collected from native cr...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1999-08, Vol.55 (8), p.1484-1486
Hauptverfasser:	Hosfield, Christopher M., Ye, Qilu, Arthur, J. Simon C., Hegadorn, Carol, Croall, Dorothy E., Elce, John S., Jia, Zongchao
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals calpain Calpain - chemistry Calpain - genetics Calpain - isolation & purification Crystallization Crystallography, X-Ray cysteine protease Dimerization Protein Conformation Rats Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Selenomethionine - chemistry
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