ArticleThe journal of physical chemistry. B2010
Determination of the phase diagram for soluble and membrane proteins.
Article in The journal of physical chemistry. B, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Investigating the Effects of Nanogels in Promoting Protein Crystallization.International journal of molecular sciences · 2026Article
- Phase Diagrams as a DOE Tool in Biomolecular Crystallization.Advances in biochemical engineering/biotechnology · 2026Review
- Quantitative Perspectives of Biomolecular Crystallization Thermodynamics.Advances in biochemical engineering/biotechnology · 2026Review
- Droplet-Based Evaporative System for the Estimation of Protein Crystallization Kinetics.Crystal growth & design · 2021Article
- Computational crystallization.Archives of biochemistry and biophysics · 2016Review
- A crystallization apparatus for temperature-controlled flow-cell dialysis with real-time visualization.Journal of applied crystallography · 2016Article
- Crystallization screening: the influence of history on current practice.Acta crystallographica. Section F, Structural biology communications · 2014Review
- Fabrication of X-ray compatible microfluidic platforms for protein crystallization.Sensors and actuators. B, Chemical · 2012Article
- A Stochastic Model for Nucleation Kinetics Determination in Droplet-Based Microfluidic Systems.Crystal growth & design · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Methods to efficiently determine the phase behavior of novel proteins have the potential to significantly benefit structural biology efforts. Here, we present protocols to determine both the solubility boundary and the supersolubility boundary for protein/precipitant systems using an evaporation-based crystallization platform. This strategy takes advantage of the well-defined rates of evaporation that occur in this platform to determine the state of the droplet at any point in time without relying on an equilibrium-based end point. The dynamic nature of this method efficiently traverses phase space along a known path, such that a solubility diagram can be mapped out for both soluble and membrane proteins while using a smaller amount of protein than what is typically used in optimization screens. Furthermore, a variation on this method can be used to decouple crystal nucleation and growth events, so fewer and larger crystals can be obtained within a given droplet. The latter protocol can be used to rescue a crystallization trial where showers of tiny crystals were observed. We validated both of the protocols to determine the phase behavior and the protocol to optimize crystal quality using the soluble proteins lysozyme and ribonuclease A as well as the membrane protein bacteriorhodopsin.
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Registered trials
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.