Soft Matter Perspective on Protein Crystal Assembly
arXiv:1505.05214 · doi:10.1016/j.colsurfb.2015.07.023
Abstract
Crystallography may be the gold standard of protein structure determination, but obtaining the necessary high-quality crystals is also in some ways akin to prospecting for the precious metal. The tools and models developed in soft matter physics to understand colloidal assembly offer some insights into the problem of crystallizing proteins. This topical review describes the various analogies that have been made between proteins and colloids in that context. We highlight the explanatory power of patchy particle models, but also the challenges of providing guidance for crystallizing specific proteins. We conclude with a presentation of possible future research directions. This article is intended for soft matter scientists interested in protein crystallization as a self-assembly problem, and as an introduction to the pertinent physics literature for protein scientists more generally.
11 pages, 3 figures, 2 table. Accepted for publication in Colloids and Surfaces B: Biointerfaces
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Cited by in corpus (12)
- The Physics of Protein Self-Assembly
- Classification of crystallization outcomes using deep convolutional neural networks
- Minimal coarse-grained models for molecular self-organisation in biology
- Real Space Analysis of Colloidal Gels: Triumphs, Challenges and Future Directions
- The physics of Empty Liquids: from Patchy particles to Water
- Minimal physical requirements for crystal growth self-poisoning
- Computational Crystallization
- Temperature-dependent non-covalent protein-protein interactions explain normal and inverted solubility in a mutant of human gamma D-crystallin
- Universal effective interactions of globular proteins close to liquid-liquid phase separation: corresponding-states behavior reflected in the structure factor
- Protein-Polymer Mixtures in the Colloid Limit: Aggregation, Sedimentation and Crystallization
- Two-step nucleation in a binary mixture of Patchy Particles
- Using schematic models to understand the microscopic basis for inverted solubility in D-crystallin