Crystallization and preliminary X-ray characterization of a novel calcium-binding protein AtCBL2 from Arabidopsis thaliana.
A new family of calcineurin B-like calcium-binding proteins has recently been identified in Arabidopsis thaliana. AtCBL2, a member of this family, has been crystallized in the presence of calcium ions using polyethylene glycol as a precipitant at 293 K. The crystals belong to space group C222(1), with unit-cell parameters a = 83.9, b = 118.1, c = 49.1 A. The asymmetric unit contains one molecule, with a V(M) of 2.36 A(3) Da(-1) and a solvent content of 48%. Native diffraction data to 2.1 A resolution have been collected using synchrotron radiation at SPring-8.
Nagae
Masamichi
M
Graduate School of Integrated Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Nozawa
Akira
A
Koizumi
Nozomu
N
Sano
Hiroshi
H
Hashimoto
Hiroshi
H
Sato
Mamoru
M
Shimizu
Toshiyuki
T
D017360:Arabidopsis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D002135:Calcium-Binding Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014961:X-Ray Diffraction
D029681:Arabidopsis Proteins; D002135:Calcium-Binding Proteins; D011994:Recombinant Proteins; C480758:At5g55990 protein, Arabidopsis