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

Fusco, Diana

Headd, Jeffrey J

De Simone, Alfonso

Wang, Jun

Charbonneau, Patrick

England

2016-08-03T15:43:28Z

2014-01-14

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.

http://www.ncbi.nlm.nih.gov/pubmed/24489597

1744-6848

https://hdl.handle.net/10161/12614

eng

Royal Society of Chemistry (RSC)

Soft Matter

10.1039/C3SM52175C

Crystallization

Molecular Dynamics Simulation

Rubredoxins

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

Journal article

Charbonneau, Patrick|0000-0001-7174-0821

http://www.ncbi.nlm.nih.gov/pubmed/24489597

290

302

2

Chemistry

Duke

Physics

Trinity College of Arts & Sciences

Published

10