PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF RECOMBINANT CALCIUM-BINDING DOMAIN OF THE SMALL-SUBUNIT OF PORCINE CALPAIN

Authors
LIN GD CHATTOPADHYAY D MAKI M TAKANO E HATANAKA M DELUCAS L NARAYANA SVL
Citation
Gd. Lin et al., PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF RECOMBINANT CALCIUM-BINDING DOMAIN OF THE SMALL-SUBUNIT OF PORCINE CALPAIN, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 474-476
Citations number
16
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
53
Year of publication
1997
Part
4
Pages
474 - 476
Database
ISI
SICI code
0907-4449(1997)53:<474:PCAPDS>2.0.ZU;2-3
Abstract
The calcium-binding domain of the small subunit of porcine calpain (do main VI) has been expressed in Escherichia coli, purified, and crystal lized in the presence of Ca2+. Two crystal forms have been obtained by the vapor-diffusion method using PEG 6000 as the precipitant. Crystal form I, belonging to trigonal space group P3(1)21 (or p3(2)21) with c ell dimensions a = b = 79.8, c = 57.08 Angstrom, alpha = beta = 90.0 a nd gamma = 120.0 degrees diffracted to 2.8 Angstrom. The second crysta l form diffracts to 1.8 Angstrom and belongs to monoclinic space group P2(1) with cell dimensions a = 50.1, b = 79.7, c = 57.1 Angstrom and beta = 91.2 degrees.