Open AccessPurification, crystallization and preliminary X‐ray diffraction studies on human Ca 2+ ‐binding protein S100B
Author(s) -
Ostendorp Thorsten,
Heizmann Claus W.,
Kroneck Peter M. H.,
Fritz Günter
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105018014
Subject(s) - dimer , extracellular , recombinant dna , crystallization , crystallography , chemistry , x ray crystallography , rage (emotion) , receptor , diffraction , biophysics , biochemistry , biology , physics , gene , neuroscience , organic chemistry , optics
S100B, a Ca 2+ ‐binding protein, acts intracellularly as a Ca 2+ ‐signalling protein but is also secreted to the extracellular space, acting in a cytokine‐like manner through its receptor RAGE. Recombinant human S100B has been purified and crystallized in the Ca 2+ ‐bound state. Size‐exclusion chromatography indicates that S100B can exist as a dimer and as a multimer in solution. Crystals of S100B diffract to 1.9 Å and belong to space group P 2 1 , with unit‐cell parameters a = 63.4, b = 81.6, c = 71.5 Å, α = 90, β = 107, γ = 90°. Preliminary analysis of the X‐ray data indicate that there are four homodimers per asymmetric unit.