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

Journal Article (Journal Article)

The fields of structural biology and soft matter have independently sought out fundamental principles to rationalize protein crystallization. Yet the conceptual differences and the limited overlap between the two disciplines have thus far prevented a comprehensive understanding of the phenomenon to emerge. We conduct a computational study of proteins from the rubredoxin family that bridges the two fields. Using atomistic simulations, we characterize the protein crystal contacts, and accordingly parameterize patchy particle models. Comparing the phase diagrams of these schematic models with experimental results enables us to critically examine the assumptions behind the two approaches. The study also reveals features of protein–protein interactions that can be leveraged to crystallize proteins more generally.

Full Text

Duke Authors

Cited Authors

  • Fusco, D; Headd, JJ; De Simone, A; Wang, J; Charbonneau, P

Published Date

  • January 2014

Published In

Volume / Issue

  • 10 / 2

Start / End Page

  • 290 - 302

PubMed ID

  • 24489597

Pubmed Central ID

  • PMC3907588

Electronic International Standard Serial Number (EISSN)

  • 1744-6848

International Standard Serial Number (ISSN)

  • 1744-683X

Digital Object Identifier (DOI)

  • 10.1039/c3sm52175c


  • eng