3ULR
Lysozyme contamination facilitates crystallization of a hetero-trimericCortactin:Arg:Lysozyme complex
3ULR の概要
| エントリーDOI | 10.2210/pdb3ulr/pdb |
| 分子名称 | Lysozyme C, Src substrate cortactin, Abelson tyrosine-protein kinase 2, ... (4 entities in total) |
| 機能のキーワード | sh3, protein-protein interaction, hydrolase, protein binding |
| 由来する生物種 | Gallus gallus (bantam,chickens) 詳細 |
| 細胞内の位置 | Cytoplasm, cytoskeleton: P00698 Q60598 Secreted: P42684 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 23403.33 |
| 構造登録者 | Liu, W.,MacGrath, S.,Koleske, A.J.,Boggon, T.J. (登録日: 2011-11-11, 公開日: 2012-01-11, 最終更新日: 2024-11-27) |
| 主引用文献 | 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 Cited by 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: 22297987DOI: 10.1107/S1744309111056132 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.65 Å) |
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