ArticleActa crystallographica. Section D, Biological crystallography2009
The role of entropy and polarity in intermolecular contacts in protein crystals.
Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- 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
- Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution.Protein science : a publication of the Protein Society · 2024Article
- A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat.Acta crystallographica. Section D, Structural biology · 2022Article
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- Designing better diffracting crystals of biotin carboxyl carrier protein from Pyrococcus horikoshii by a mutation based on the crystal-packing propensity of amino acids.Acta crystallographica. Section D, Structural biology · 2017Article
- The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Methods in molecular biology (Clifton, N.J.) · 2017Review
- Computational crystallization.Archives of biochemistry and biophysics · 2016Review
- The role of flexibility and molecular shape in the crystallization of proteins by surface mutagenesis.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Effects of protein engineering and rational mutagenesis on crystal lattice of single chain antibody fragments.Proteins · 2014Article
- Characterizing protein crystal contacts and their role in crystallization: rubredoxin as a case study.Soft matter · 2014Article
- Statistical analysis of crystallization database links protein physico-chemical features with crystallization mechanisms.PloS one · 2014Article
- Cellular crowding imposes global constraints on the chemistry and evolution of proteomes.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- An approach to crystallizing proteins by metal-mediated synthetic symmetrization.Protein science : a publication of the Protein Society · 2011Article
- It's all in the crystals….Acta crystallographica. Section D, Biological crystallography · 2011Article
- Abstractions, algorithms and data structures for structural bioinformatics in PyCogent.Journal of applied crystallography · 2011Article
- Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Application of protein engineering to enhance crystallizability and improve crystal properties.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Introduction of a leucine half-zipper engenders multiple high-quality crystals of a recalcitrant tRNA synthetase.Acta crystallographica. Section D, Biological crystallography · 2010Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The integrity and X-ray diffraction quality of protein crystals depend on the three-dimensional order of relatively weak but reproducible intermolecular contacts. Despite their importance, relatively little attention has been paid to the chemical and physical nature of these contacts, which are often regarded as stochastic and thus not different from randomly selected protein surface patches. Here, logistic regression was used to analyze crystal contacts in a database of 821 unambiguously monomeric proteins with structures determined to 2.5 A resolution or better. It is shown that the propensity of a surface residue for incorporation into a crystal contact is not a linear function of its solvent-accessible surface area and that amino acids with low exposed surfaces, which are typically small and hydrophobic, have been underestimated with respect to their contact-forming potential by earlier area-based calculations. For any given solvent-exposed surface, small and hydrophobic residues are more likely to be involved in crystal contacts than large and charged amino acids. Side-chain entropy is the single physicochemical property that is most negatively correlated with the involvement of amino acids in crystal contacts. It is also shown that crystal contacts with larger buried surfaces containing eight or more amino acids have cores that are depleted of polar amino acids.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.