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

Christopher M. Hosfield, Qilu Ye, J. Simon C. Arthur, Carol Hegadorn, Dorothy E. Croall, John S. Elce, Zongchao Jia

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


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 crystals of m-calpain in both P1 and P21 forms, to 2.6 and 2.15 Å, respectively. Selenomethionine-containing crystals have been grown in both forms, and anomalous data from the P21 selenomethionine enzyme provided the location of 17 of the 19 Se atoms in the protein.

Original languageEnglish
Pages (from-to)1484-1486
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Issue number8
Publication statusPublished - Aug 1999

ASJC Scopus subject areas

  • Structural Biology


Dive into the research topics of 'Crystallization and X-ray crystallographic analysis of m-calpain, a Ca2+-dependent protease'. Together they form a unique fingerprint.

Cite this