ArticleActa crystallographica. Section D, Structural biology2020
The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography.
Article in Acta crystallographica. Section D, Structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 7 citations in OpenAlex.
- Structure-Based Understanding of CuBiosensors · 2025Review
- Topically applied GHK as an anti-wrinkle peptide: Advantages, problems and prospective.BioImpacts : BI · 2025Review
- Glycyl-l-histidyl-l-lysine prevents copper- and zinc-induced protein aggregation and central nervous system cell death in vitro.Metallomics : integrated biometal science · 2024Article
- IndiumJournal of applied crystallography · 2023Article
- Structural basis for lipid and copper regulation of the ABC transporter MsbA.Nature communications · 2022Article
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5 authors at 1 institution in 1 country.
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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.
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