6QUJ
GHK tagged GFP variant
Summary for 6QUJ
| Entry DOI | 10.2210/pdb6quj/pdb |
| Related | 6QUG 6QUH 6QUI |
| Descriptor | Green fluorescent protein, COPPER (II) ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | gfp, fluorescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 2 |
| Total formula weight | 53266.17 |
| Authors | Huyton, T.,Gorlich, D. (deposition date: 2019-02-27, release date: 2020-05-27, Last modification date: 2024-10-09) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.68 Å) |
Structure validation
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