Crystallization and preliminary X-ray diffraction data of the complex between human centrin 2 and a peptide from the protein XPC
- Laboratoire de Structure des Protéines, Département d’Ingénierie et d’Étude des Protéines, Commissariat à l’Energie Atomique CEA, 91191 Gif-sur-Yvette (France)
- Institute of Organic Chemistry, Bulgarian Academy of Sciences, Sofia (Bulgaria)
Production, crystallization and phasing procedures are reported for the complex of human centrin 2, lacking the first 25 residues, and a 17-residue peptide from the protein XPC. Centrins are highly conserved calcium-binding proteins involved in the nucleotide-excision repair pathway as a subunit of the heterotrimer including the XPC and hHR23B proteins. A complex formed by a Ca{sup 2+}-bound human centrin 2 construct (the wild type lacking the first 25 amino acids) with a 17-mer peptide derived from the XPC sequence (residues Asn847–Arg863) was crystallized. Data were collected to 1.65 Å resolution from crystals grown in 30% monomethyl polyethylene glycol (MPEG) 500, 100 mM NaCl and 100 mM Bicine pH 9.0. Crystals are monoclinic and belong to space group C2, with two molecules in the asymmetric unit. The unit-cell parameters are a = 60.28, b = 59.42, c = 105.14 Å, α = γ = 90, β = 94.67°. A heavy-atom derivative was obtained by co-crystallization with Sr{sup 2+}. The substitution was rationalized by calorimetry experiments, which indicate a binding constant for Sr{sup 2+} of 4.0 × 10{sup 4} M{sup −1}.
- OSTI ID:
- 22360205
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 7; Other Information: PMCID: PMC2242955; PMID: 16820684; PUBLISHER-ID: hc5004; OAI: oai:pubmedcentral.nih.gov:2242955; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin
Crystallization and preliminary X-ray studies of mouse centrin1