ArticleProtein science : a publication of the Protein Society2007
'Crystal lattice engineering,' an approach to engineer protein crystal contacts by creating intermolecular symmetry: crystallization and structure determination of a mutant human RNase 1 with a hydrophobic interface of leucines.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed.
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- Time-series analysis of rhenium(I) organometallic covalent binding to a model protein for drug development.IUCrJ · 2024Article
- Domino-like effect of C112R mutation on ApoE4 aggregation and its reduction by Alzheimer's Disease drug candidate.Molecular neurodegeneration · 2023Article
- Creation of Cross-Linked Crystals With Intermolecular Disulfide Bonds Connecting Symmetry-Related Molecules Allows Retention of Tertiary Structure in Different Solvent Conditions.Frontiers in molecular biosciences · 2022Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Co-crystallization with diabodies: A case study for the introduction of synthetic symmetry.Structure (London, England : 1993) · 2021Article
- On the irrationality of rational design of an HIV vaccine in light of protein intrinsic disorder.Archives of virology · 2021Review
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- Development of imaging scaffolds for cryo-electron microscopy.Current opinion in structural biology · 2020Review
- Lattice engineering enables definition of molecular features allowing for potent small-molecule inhibition of HIV-1 entry.Nature communications · 2019Article
- Structural basis for recognition of human 7SK long noncoding RNA by the La-related protein Larp7.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural analysis of β-glucosidase mutants derived from a hyperthermophilic tetrameric structure.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Split green fluorescent protein as a modular binding partner for protein crystallization.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Surface reengineering of RPA70N enables cocrystallization with an inhibitor of the replication protein A interaction motif of ATR interacting protein.Biochemistry · 2013Article
- Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Computational design of a protein crystal.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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- An approach to crystallizing proteins by metal-mediated synthetic symmetrization.Protein science : a publication of the Protein Society · 2011Article
- Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima.Protein science : a publication of the Protein Society · 2011Article
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Abstract
A protein crystal lattice consists of surface contact regions, where the interactions of specific groups play a key role in stabilizing the regular arrangement of the protein molecules. In an attempt to control protein incorporation in a crystal lattice, a leucine zipper-like hydrophobic interface (comprising four leucine residues) was introduced into a helical region (helix 2) of the human pancreatic ribonuclease 1 (RNase 1) that was predicted to form a suitable crystallization interface. Although crystallization of wild-type RNase 1 has not yet been reported, the RNase 1 mutant having four leucines (4L-RNase 1) was successfully crystallized under several different conditions. The crystal structures were subsequently determined by X-ray crystallography by molecular replacement using the structure of bovine RNase A. The overall structure of 4L-RNase 1 is quite similar to that of the bovine RNase A, and the introduced leucine residues formed the designed crystal interface. To characterize the role of the introduced leucine residues in crystallization of RNase 1 further, the number of leucines was reduced to three or two (3L- and 2L-RNase 1, respectively). Both mutants crystallized and a similar hydrophobic interface as in 4L-RNase 1 was observed. A related approach to engineer crystal contacts at helix 3 of RNase 1 (N4L-RNase 1) was also evaluated. N4L-RNase 1 also successfully crystallized and formed the expected hydrophobic packing interface. These results suggest that appropriate introduction of a leucine zipper-like hydrophobic interface can promote intermolecular symmetry for more efficient protein crystallization in crystal lattice engineering efforts.
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