N-terminal t4 lysozyme fusion facilitates crystallization of a g protein coupled receptor.
Zou, Y., Weis, W.I., Kobilka, B.K.(2012) PLoS One 7: e46039-e46039
- PubMed: 23056231 
- DOI: https://doi.org/10.1371/journal.pone.0046039
- Primary Citation of Related Structures:  
4GBR - PubMed Abstract: 
A highly crystallizable T4 lysozyme (T4L) was fused to the N-terminus of the ¦Â(2) adrenergic receptor (¦Â(2)AR), a G-protein coupled receptor (GPCR) for catecholamines. We demonstrate that the N-terminal fused T4L is sufficiently rigid relative to the receptor to facilitate crystallogenesis without thermostabilizing mutations or the use of a stabilizing antibody, G protein, or protein fused to the 3rd intracellular loop. This approach adds to the protein engineering strategies that enable crystallographic studies of GPCRs alone or in complex with a signaling partner.
Organizational Affiliation: 
Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California, United States of America.