Crystallization and Preliminary Crystallographic Analysis of Human Ca 2+-loaded Calbindin-D28k

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2008 Feb 9

PMID 18259068

Citations 2

Authors

Chang Zhang

Yuna Sun

Wei Wang

Yan Zhang

Ming Ma

Zhiyong Lou

Affiliations

Soon will be listed here.

Abstract

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 A resolution X-ray data set was collected from a single flash-cooled crystal (100 K). The crystal belonged to space group C2, with unit-cell parameters a = 108.1, b = 28.2, c = 70.6 A, beta = 107.8 degrees . The presence of one molecule per asymmetric unit is presumed, corresponding to a Matthews coefficient of 1.75 A(3) Da(-1).

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