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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt 2):154-8. doi: 10.1107/S1744309111056132. Epub 2012 Jan 25.

Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex.

Author information

1
Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA.

Abstract

Crystallization of contaminating proteins is a frequently encountered problem for macromolecular crystallographers. In this study, an attempt was made to obtain a binary cocrystal structure of the SH3 domain of cortactin and a 17-residue peptide from the Arg nonreceptor tyrosine kinase encompassing a PxxPxxPxxP (PxxP1) motif. However, cocrystals could only be obtained in the presence of trace amounts of a contaminating protein. A structure solution obtained by molecular replacement followed by ARP/wARP automatic model building allowed a 'sequence-by-crystallography' approach to discover that the contaminating protein was lysozyme. This 1.65 Å resolution crystal structure determination of a 1:1:1 heterotrimeric complex of Arg, cortactin and lysozyme thus provides an unusual `caveat emptor' warning of the dangers that underpurified proteins harbor for macromolecular crystallographers.

PMID:
22297987
PMCID:
PMC3274391
DOI:
10.1107/S1744309111056132
[Indexed for MEDLINE]
Free PMC Article

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