Open AccessPurification and crystallization of the human EF‐hand tumour suppressor protein S100A2
Author(s) -
Koch Michael,
Diez Joachim,
Fritz Günter
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106039881
Subject(s) - mutant , crystallization , crystallography , nucleus , wild type , suppressor , chemistry , beta (programming language) , microbiology and biotechnology , biophysics , stereochemistry , biology , biochemistry , gene , organic chemistry , computer science , programming language
S100A2 is a Ca 2+ ‐binding EF‐hand protein that is mainly localized in the nucleus. There, it acts as a tumour suppressor by binding and activating p53. Wild‐type S100A2 and a S100A2 variant lacking cysteines have been purified. CD spectroscopy showed that there are no changes in secondary‐structure composition. The S100A2 mutant was crystallized in a calcium‐free form. The crystals, with dimensions 30 × 30 × 70 µm, diffract to 1.7 Å and belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 43.5, b = 57.8, c = 59.8 Å, α = β = γ = 90°. Preliminary analysis of the X‐ray data indicates that there are two subunits per asymmetric unit.