title: X-ray structural analysis of S100 proteins.
abstract: X-ray crystallography is a potent and meanwhile fast technique to obtain detailed structural information of S100 proteins in their apo or metal ion-loaded state. S100 proteins crystallize in the absence or presence of Ca(2+) and Zn(2+) and the obtained crystals often diffract to high resolution yielding information on the ion-binding sites, conformation, and target interaction sites of the proteins. Here, I describe a general scheme to isolate and crystallize S100 proteins and the analysis of protein crystals using a modern synchrotron source.
authors.affiliation: Department of Neuropathology, Neurozentrum, University of Freiburg, Freiburg, Germany. guenter.fritz@uniklinik-freiburg.de
authors.forename: Günter
authors.initials: G
authors.lastname: Fritz
mesh_terms: D020816:Amino Acid Motifs; D001059:Apoproteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods*; D004926:Escherichia coli / Q000235:genetics; D008958:Models, Molecular; D009418:S100 Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D017356:Synchrotrons
chemical_list: D001059:Apoproteins; D009418:S100 Proteins