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Updated: Sep 25, 2026

Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
Crystallization and preliminary X-ray characterization of a novel calcium-binding protein AtCBL2 from Arabidopsis
Masamichi Nagae1, Akira Nozawa, Nozomu Koizumi
1Graduate School of Integrated Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Abstract:
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.

