English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The fields of structural biology and soft matter have independently soughtout fundamental principles to rationalize protein crystallization. Yet theconceptual differences and the limited overlap between the two disciplines havethus far prevented a comprehensive understanding of the phenomenon to emerge.We conduct a computational study of proteins from the rubredoxin family thatbridges the two fields. Using atomistic simulations, we characterize theircrystal contacts, and accordingly parameterize patchy particle models.Comparing the phase diagrams of these schematic models with experimentalresults enables us to critically examine the assumptions behind the twoapproaches. The study also reveals features of protein-protein interactionsthat can be leveraged to crystallize proteins more generally.

Characterizing protein crystal contacts and their role in crystallization: rubredoxin as a case study