ArticleCrystal growth & design2014
Polymorphic Protein Crystal Growth: Influence of Hydration and Ions in Glucose Isomerase.
Article in Crystal growth & design, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Quantitative Perspectives of Biomolecular Crystallization Thermodynamics.Advances in biochemical engineering/biotechnology · 2026Review
- Protein-macrocycle polymorphism: crystal form IV of the Ralstonia solanacearum lectin-sulfonato-calix[8]arene complex.Acta crystallographica. Section D, Structural biology · 2023Article
- Article
- Nucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Molecular nucleation mechanisms and control strategies for crystal polymorph selection.Nature · 2018Article
- Observing classical nucleation theory at work by monitoring phase transitions with molecular precision.Nature communications · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Crystal polymorphs of glucose isomerase were examined to characterize the properties and to quantify the energetics of protein crystal growth. Transitions of polymorph stability were measured in poly(ethylene glycol)/NaCl solutions, and one transition point was singled out for more detailed quantitative analysis. Single crystal x-ray diffraction was used to confirm space groups and identify complementary crystal structures. Crystal polymorph stability was found to depend on the NaCl concentration, with stability transitions requiring > 1 M NaCl combined with a low concentration of PEG. Both salting-in and salting-out behavior was observed and was found to differ for the two polymorphs. For NaCl concentrations above the observed polymorph transition, the increase in solubility of the less stable polymorph together with an increase in the osmotic second virial coefficient suggests that changes in protein hydration upon addition of salt may explain the experimental trends. A combination of atomistic and continuum models was employed to dissect this behavior. Molecular dynamics simulations of the solvent environment were interpreted using quasi-chemical theory to understand changes in protein hydration as a function of NaCl concentration. The results suggest that protein surface hydration and Na
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Registered trials
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