TY - JOUR
T1 - Crystallization and X-ray crystallographic analysis of m-calpain, a Ca2+-dependent protease
AU - Hosfield, Christopher M.
AU - Ye, Qilu
AU - Arthur, J. Simon C.
AU - Hegadorn, Carol
AU - Croall, Dorothy E.
AU - Elce, John S.
AU - Jia, Zongchao
PY - 1999/8
Y1 - 1999/8
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033180293&partnerID=8YFLogxK
U2 - 10.1107/S0907444999007386
DO - 10.1107/S0907444999007386
M3 - Article
C2 - 10417423
AN - SCOPUS:0033180293
SN - 0907-4449
VL - 55
SP - 1484
EP - 1486
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 8
ER -