ArticleProtein science : a publication of the Protein Society2011
An approach to crystallizing proteins by metal-mediated synthetic symmetrization.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Structure-Based Understanding of CuBiosensors · 2025Review
- Nickel binding to c-Src SH3 domain facilitates crystallization.bioRxiv : the preprint server for biology · 2025Article
- Nickel Binding to the c-Src SH3 Domain Facilitates Crystallization.Protein and peptide letters · 2025Article
- Grafting the ALFA tag for structural studies of aquaporin Z.Journal of structural biology: X · 2024Article
- Polymorphic nanobody crystals as long-acting intravitreal therapy for wet age-related macular degeneration.Bioengineering & translational medicine · 2023Article
- mebipred: identifying metal-binding potential in protein sequence.Bioinformatics (Oxford, England) · 2022Article
- 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
- Protein Assembly by Design.Chemical reviews · 2021Review
- Redefining Protein Interfaces within Protein Single Crystals with DNA.Journal of the American Chemical Society · 2021Article
- Co-crystallization with diabodies: A case study for the introduction of synthetic symmetry.Structure (London, England : 1993) · 2021Article
- The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2020Article
- Structure of the RECK CC domain, an evolutionary anomaly.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural underpinnings of Ric8A function as a G-protein α-subunit chaperone and guanine-nucleotide exchange factor.Nature communications · 2019Article
- T4 lysozyme-facilitated crystallization of the human molybdenum cofactor-dependent enzyme mARC.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Modular assembly of a protein nanotriangle using orthogonally interacting coiled coils.Scientific reports · 2017Article
- Can the propensity of protein crystallization be increased by using systematic screening with metals?Protein science : a publication of the Protein Society · 2017Review
- Benchmarking a computational design method for the incorporation of metal ion-binding sites at symmetric protein interfaces.Protein science : a publication of the Protein Society · 2017Article
- Review
- Design of an expression system to enhance MBP-mediated crystallization.Scientific reports · 2017Article
- The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Methods in molecular biology (Clifton, N.J.) · 2017Review
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6 authors.
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Abstract
Combining the concepts of synthetic symmetrization with the approach of engineering metal-binding sites, we have developed a new crystallization methodology termed metal-mediated synthetic symmetrization. In this method, pairs of histidine or cysteine mutations are introduced on the surface of target proteins, generating crystal lattice contacts or oligomeric assemblies upon coordination with metal. Metal-mediated synthetic symmetrization greatly expands the packing and oligomeric assembly possibilities of target proteins, thereby increasing the chances of growing diffraction-quality crystals. To demonstrate this method, we designed various T4 lysozyme (T4L) and maltose-binding protein (MBP) mutants and cocrystallized them with one of three metal ions: copper (Cu²⁺, nickel (Ni²⁺), or zinc (Zn²⁺). The approach resulted in 16 new crystal structures--eight for T4L and eight for MBP--displaying a variety of oligomeric assemblies and packing modes, representing in total 13 new and distinct crystal forms for these proteins. We discuss the potential utility of the method for crystallizing target proteins of unknown structure by engineering in pairs of histidine or cysteine residues. As an alternate strategy, we propose that the varied crystallization-prone forms of T4L or MBP engineered in this work could be used as crystallization chaperones, by fusing them genetically to target proteins of interest.
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