ArticleActa crystallographica. Section D, Biological crystallography2010
Application of protein engineering to enhance crystallizability and improve crystal properties.
Article in Acta crystallographica. Section D, Biological crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed.
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- Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Polo-like kinase 1-inhibitor co-complex structures via the surface-entropy reduction approach and a DARPin-assisted approach.Acta crystallographica. Section D, Structural biology · 2025Article
- Optimal TELSAM-Target Protein Linker Character is Target Protein-Dependent.bioRxiv : the preprint server for biology · 2025Article
- A generic cross-seeding approach to protein crystallization.Journal of applied crystallography · 2025Article
- Antigen-binding fragments with improved crystal lattice packing and enhanced conformational flexibility at the elbow region as crystallization chaperones.Protein science : a publication of the Protein Society · 2024Article
- Structural studies of intrinsically disordered MLL-fusion protein AF9 in complex with peptidomimetic inhibitors.Protein science : a publication of the Protein Society · 2024Article
- Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes.Protein science : a publication of the Protein Society · 2024Article
- A scalable overexpression of a thermostable recombinant poly-histidine tag carboxyl esterase under lambda promoter: purification, characterization, and protein modelling.Journal, genetic engineering & biotechnology · 2023Article
- Influence of HIV-1 Genomic RNA on the Formation of Gag Biomolecular Condensates.Journal of molecular biology · 2023Article
- Nonspecific Binding of Adenosine Tripolyphosphate and Tripolyphosphate Modulates the Phase Behavior of Lysozyme.Journal of the American Chemical Society · 2023Article
- Structure-based engineering of minimal proline dehydrogenase domains for inhibitor discovery.Protein engineering, design & selection : PEDS · 2022Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Nuclear compartmentalization as a mechanism of quantitative control of gene expression.Nature reviews. Molecular cell biology · 2021Review
- Co-crystallization with diabodies: A case study for the introduction of synthetic symmetry.Structure (London, England : 1993) · 2021Article
- Characterization of binding kinetics of ABiophysical journal · 2021Article
- Article
- Development of imaging scaffolds for cryo-electron microscopy.Current opinion in structural biology · 2020Review
- In Situ Proteolysis Condition-Induced Crystallization of the XcpVWX Complex in Different Lattices.International journal of molecular sciences · 2020Article
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Abstract
Until recently, protein crystallization has mostly been regarded as a stochastic event over which the investigator has little or no control. With the dramatic technological advances in synchrotron-radiation sources and detectors and the equally impressive progress in crystallographic software, including automated model building and validation, crystallization has increasingly become the rate-limiting step in X-ray diffraction studies of macromolecules. However, with the advent of recombinant methods it has also become possible to engineer target proteins and their complexes for higher propensity to form crystals with desirable X-ray diffraction qualities. As most proteins that are under investigation today are obtained by heterologous overexpression, these techniques hold the promise of becoming routine tools with the potential to transform classical crystallization screening into a more rational high-success-rate approach. This article presents an overview of protein-engineering methods designed to enhance crystallizability and discusses a number of examples of their successful application.
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