title: Expression, refolding and crystallization of Aquifex aeolicus elongation factor P.
abstract: Elongation factor P is a universally conserved protein stimulating peptidyltransferase activity during protein synthesis. The factor is sensitive to classical inhibitors of the ribosomal peptidyltransferase activity and is possibly involved in alignment of the substrate tRNAs in the catalytic centre of 70S ribosomes. Elongation factor P from the thermophilic Aquifex aeolicus was overexpressed as a soluble protein in Escherichia coli and crystallized. A fast generally applicable refolding protocol was developed to improve crystal quality and circumvent strong binding of oligonucleotides to the protein. Diffraction data collected to 2.7 A resolution present twinning.
authors.affiliation: Protein Structure Group, Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark. olek@psg.ki.ku.dk
authors.forename: Ole
authors.initials: O
authors.lastname: Kristensen
authors.forename: Martin
authors.initials: M
authors.lastname: Laurberg
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D010445:Peptide Elongation Factors / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D001426:Bacterial Proteins; D010445:Peptide Elongation Factors; C020746:factor EF-P