Open AccessCrystallization and preliminary crystallographic analysis of human Ca 2+ ‐loaded calbindin‐D28k
Author(s) -
Zhang Chang,
Sun Yuna,
Wang Wei,
Zhang Yan,
Ma Ming,
Lou Zhiyong
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108001905
Subject(s) - crystallization , crystallography , calbindin , calcium binding protein , calcium , chemistry , recombinant dna , crystal structure , biology , biochemistry , organic chemistry , gene
Calbindin‐D28k is a calcium‐binding protein that belongs to the troponin C superfamily. It is expressed in many tissues, including brain, intestine, kidney and pancreas, and performs roles as both a calcium buffer and a calcium sensor and carries out diverse physiological functions of importance. In order to resolve the crystal structure of human calbindin‐D28k and to gain a better understanding of its biological functions, recombinant human calbindin‐D28k was crystallized at 291 K using PEG 3350 as precipitant and a 2.4 Å resolution X‐ray data set was collected from a single flash‐cooled crystal (100 K). The crystal belonged to space group C 2, with unit‐cell parameters a = 108.1, b = 28.2, c = 70.6 Å, β = 107.8°. The presence of one molecule per asymmetric unit is presumed, corresponding to a Matthews coefficient of 1.75 Å 3 Da −1 .