ArticleScientific reports2019
Structural analysis of biological targets by host:guest crystal lattice engineering.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Modular protein frameworks via supramolecular synthons.Biophysical reviews · 2025Review
- Tuning Chemical DNA Ligation within DNA Crystals and Protein-DNA Cocrystals.ACS nanoscience Au · 2024Article
- A suite of designed protein cages using machine learning and protein fragment-based protocols.Structure (London, England : 1993) · 2024Article
- A Suite of Designed Protein Cages Using Machine Learning Algorithms and Protein Fragment-Based Protocols.bioRxiv : the preprint server for biology · 2023Article
- Increasing the bulk of the 1TEL-target linker and retaining the 10×His tag in a 1TEL-CMG2-vWa construct improves crystal order and diffraction limits.Acta crystallographica. Section D, Structural biology · 2023Article
- Supramolecular Assembly of His-Tagged Fluorescent Protein Guests within Coiled-Coil Peptide Crystal Hosts: Three-Dimensional Ordering and Protein Thermal Stability.ACS biomaterials science & engineering · 2022Article
- Review
- A fragment-based protein interface design algorithm for symmetric assemblies.Protein engineering, design & selection : PEDS · 2021Article
- C-phycocyanin as a highly attractive model system in protein crystallography: unique crystallization properties and packing-diversity screening.Acta crystallographica. Section D, Structural biology · 2021Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To overcome the laborious identification of crystallisation conditions for protein X-ray crystallography, we developed a method where the examined protein is immobilised as a guest molecule in a universal host lattice. We applied crystal engineering to create a generic crystalline host lattice under reproducible, predefined conditions and analysed the structures of target guest molecules of different size, namely two 15-mer peptides and green fluorescent protein (sfGFP). A fusion protein with an N-terminal endo-α-N-acetylgalactosaminidase (EngBF) domain and a C-terminal designed ankyrin repeat protein (DARPin) domain establishes the crystal lattice. The target is recruited into the host lattice, always in the same crystal form, through binding to the DARPin. The target structures can be determined rapidly from difference Fourier maps, whose quality depends on the size of the target and the orientation of the DARPin.
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