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Ca^2+^‐Binding domain VI of rat calpain is a homodimer in solution: Hydrodynamic, crystallization and preliminary X‐ray diffraction studies by Helen Blanchard; Yunge Li; Miroslaw Cygler; Cyril M. Kay; J. Simon C. Arthur; Peter L. Davies; John S. Elce is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Ca^2+^‐Binding domain VI of rat calpain is a homodimer in solution: Hydrodynamic, crystallization and preliminary X‐ray diffraction studies about?

## Abstract Abstract: The 21‐kDa calcium‐binding domain (VI) of the small subunit of rat calpain II has been expressed in __Escherichia coli__, purified, and crystallized. Two orthorhombic crystal forms have been obtained: space group P2~1~2~1~2~1~ with __a__ = 50.3, __b__ = 56.5, __c__ = 141.3 Å; and space group C222~1~ with __a__ = 69.4, __b__ = 73.9, __c__ = 157.4 Å. Diffraction data have been collected to 2.4 Å. Sedimentation equilibrium, dynamic light scattering, and gel‐permeation chromatography indicate that domain VI exists as a homodimer in solution. In accordance with the protein's behavior in solution, each crystal form contains two molecules per asymmetric unit. Screening for heavy‐atom derivatives is in progress. To decrease the sensitivity to mercurials and to aid in the search for useful derivatives, Cys‐to‐Ser mutants have been prepared, expressed, and crystallized.

Who reads Ca^2+^‐Binding domain VI of rat calpain is a homodimer in solution: Hydrodynamic, crystallization and preliminary X‐ray diffraction studies?

Author

Helen Blanchard; Yunge Li; Miroslaw Cygler; Cyril M. Kay; J. Simon C. Arthur; Peter L. Davies; John S. Elce

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)