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Updated: Jul 12, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Expression, purification, crystallization and preliminary crystallographic analysis of the proliferation-associated
Eva Kowalinski1, Gert Bange, Klemens Wild
1Heidelberg University Biochemistry Center, INF 328, D-69120 Heidelberg, Germany.
Abstract:
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(1)2(1)2 or P4(3)2(1)2 and diffracted to a resolution of 1.6 A.

