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Soft matter perspective on protein crystal assembly.

dc.contributor.author Charbonneau, Patrick
dc.contributor.author Fusco, Diana
dc.coverage.spatial Netherlands
dc.date.accessioned 2017-08-23T15:44:07Z
dc.date.available 2017-08-23T15:44:07Z
dc.date.issued 2016-01-01
dc.identifier https://www.ncbi.nlm.nih.gov/pubmed/26236019
dc.identifier S0927-7765(15)30057-6
dc.identifier.uri https://hdl.handle.net/10161/15338
dc.description.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 review 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.
dc.language eng
dc.relation.ispartof Colloids Surf B Biointerfaces
dc.relation.isversionof 10.1016/j.colsurfb.2015.07.023
dc.subject Patchy particle models
dc.subject Protein crystallization
dc.subject Protein phase diagram
dc.subject Crystallization
dc.subject Crystallography
dc.subject Proteins
dc.subject Solubility
dc.title Soft matter perspective on protein crystal assembly.
dc.type Journal article
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/26236019
pubs.begin-page 22
pubs.end-page 31
pubs.organisational-group Chemistry
pubs.organisational-group Duke
pubs.organisational-group Physics
pubs.organisational-group Trinity College of Arts & Sciences
pubs.publication-status Published
pubs.volume 137
dc.identifier.eissn 1873-4367


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