6QUJ
GHK tagged GFP variant
6QUJ の概要
| エントリーDOI | 10.2210/pdb6quj/pdb |
| 関連するPDBエントリー | 6QUG 6QUH 6QUI |
| 分子名称 | Green fluorescent protein, COPPER (II) ION, SULFATE ION, ... (5 entities in total) |
| 機能のキーワード | gfp, fluorescent protein |
| 由来する生物種 | Aequorea victoria |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 53266.17 |
| 構造登録者 | |
| 主引用文献 | Mehr, A.,Henneberg, F.,Chari, A.,Gorlich, D.,Huyton, T. The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography. Acta Crystallogr D Struct Biol, 76:1222-1232, 2020 Cited by PubMed Abstract: The growth of diffraction-quality crystals and experimental phasing remain two of the main bottlenecks in protein crystallography. Here, the high-affinity copper(II)-binding tripeptide GHK was fused to the N-terminus of a GFP variant and an MBP-FG peptide fusion. The GHK tag promoted crystallization, with various residues (His, Asp, His/Pro) from symmetry molecules completing the copper(II) square-pyramidal coordination sphere. Rapid structure determination by copper SAD phasing could be achieved, even at a very low Bijvoet ratio or after significant radiation damage. When collecting highly redundant data at a wavelength close to the copper absorption edge, residual S-atom positions could also be located in log-likelihood-gradient maps and used to improve the phases. The GHK copper SAD method provides a convenient way of both crystallizing and phasing macromolecular structures, and will complement the current trend towards native sulfur SAD and MR-SAD phasing. PubMed: 33263328DOI: 10.1107/S2059798320013741 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.68 Å) |
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