Crystallization and preliminary crystallographic analysis of human Ca{sup 2+}-loaded calbindin-D28k
- Tsinghua-Nankai-IBP Joint Research Group for Structural Biology, Tsinghua University, Beijing 100084 (China)
- National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101 (China)
Human calbindin-D28k has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.4 Å resolution. 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 C2, 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{sup 3} Da{sup −1}.
- OSTI ID:
- 22360495
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 2; Other Information: PMCID: PMC2374171; PMID: 18259068; PUBLISHER-ID: en5282; OAI: oai:pubmedcentral.nih.gov:2374171; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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