Expression, purification, crystallization and preliminary crystallographic analysis of the proliferation-associated protein Ebp1
- Heidelberg University Biochemistry Center, INF 328, D-69120 Heidelberg (Germany)
Preliminary X-ray analysis of the proliferation-associated protein Ebp1 from Homo sapiens is provided. ErbB-3-binding protein 1 (Ebp1) is a member of the family of proliferation-associated 2G4 proteins (PA2G4s) and plays a role in cellular growth and differentiation. Ligand-induced activation of the transmembrane receptor ErbB3 leads to dissociation of Ebp1 from the receptor in a phosphorylation-dependent manner. The non-associated protein is involved in transcriptional and translational regulation in the cell. Here, the overexpression, purification, crystallization and preliminary crystallographic studies of Ebp1 from Homo sapiens are reported. Initially observed crystals were improved by serial seeding to single crystals suitable for data collection. The optimized crystals belong to the tetragonal space group P4{sub 1}2{sub 1}2 or P4{sub 3}2{sub 1}2 and diffracted to a resolution of 1.6 Å.
- OSTI ID:
- 22360536
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 9; Other Information: PMCID: PMC2376314; PMID: 17768350; PUBLISHER-ID: gj5026; OAI: oai:pubmedcentral.nih.gov:2376314; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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