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X-ray structural analysis of S100 proteins.
- Source :
-
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2013; Vol. 963, pp. 87-97. - Publication Year :
- 2013
-
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.
- Subjects :
- Amino Acid Motifs
Apoproteins chemistry
Apoproteins genetics
Apoproteins isolation & purification
Crystallography, X-Ray instrumentation
Escherichia coli genetics
Models, Molecular
S100 Proteins genetics
S100 Proteins isolation & purification
Synchrotrons
Crystallography, X-Ray methods
S100 Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1940-6029
- Volume :
- 963
- Database :
- MEDLINE
- Journal :
- Methods in molecular biology (Clifton, N.J.)
- Publication Type :
- Academic Journal
- Accession number :
- 23296606
- Full Text :
- https://doi.org/10.1007/978-1-62703-230-8_6