3ULR

Lysozyme contamination facilitates crystallization of a hetero-trimericCortactin:Arg:Lysozyme complex

Summary for 3ULR

• Entry DOI: 10.2210/pdb3ulr/pdb
• Descriptor: Lysozyme C, Src substrate cortactin, Abelson tyrosine-protein kinase 2, ... (4 entities in total)
• Functional Keywords: sh3, protein-protein interaction, hydrolase, protein binding
• Biological source: Gallus gallus (bantam,chickens); More
• Cellular location: Cytoplasm, cytoskeleton: P00698 Q60598; Secreted: P42684
• Total number of polymer chains: 3
• Total formula weight: 23403.33

Authors

Liu, W.,MacGrath, S.,Koleske, A.J.,Boggon, T.J. (deposition date: 2011-11-11, release date: 2012-01-11, Last modification date: 2024-11-27)

Primary citation

Liu, W.,Macgrath, S.M.,Koleske, A.J.,Boggon, T.J.
Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex.
Acta Crystallogr.,Sect.F, 68:154-158, 2012

PubMed 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.

PubMed: 22297987
DOI: 10.1107/S1744309111056132

Experimental method

X-RAY DIFFRACTION (1.65 Å)