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

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 - https://www.scopus.com/pages/publications/0033180293

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 -