scholarly journals Structure determination of membrane proteins in five easy pieces

Methods ◽  
2011 ◽  
Vol 55 (4) ◽  
pp. 363-369 ◽  
Author(s):  
Francesca M. Marassi ◽  
Bibhuti B. Das ◽  
George J. Lu ◽  
Henry J. Nothnagel ◽  
Sang Ho Park ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Structure Determination

scholarly journals Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins

FEBS Letters ◽  
2010 ◽  
Vol 584 (12) ◽  
pp. 2539-2547 ◽  
Author(s):  
Yo Sonoda ◽  
Alex Cameron ◽  
Simon Newstead ◽  
Hiroshi Omote ◽  
Yoshinori Moriyama ◽  
...  
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Structure Determination ◽  
High Resolution Structure ◽  
Resolution Structure

scholarly journals Structure Determination of Membrane Proteins in Five Easy Pieces

2012 ◽  
Vol 102 (3) ◽  
pp. 390a-391a
Author(s):  
Ye Tian ◽  
Francesca M. Marassi ◽  
Bibhuti B. Das ◽  
George J. Lu ◽  
Henry J. Nothnagel ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Structure Determination

scholarly journals Femtosecond crystallography of membrane proteins in the lipidic cubic phase

2014 ◽  
Vol 369 (1647) ◽  
pp. 20130314 ◽  
Author(s):  
Wei Liu ◽  
Daniel Wacker ◽  
Chong Wang ◽  
Enrique Abola ◽  
Vadim Cherezov
Keyword(s):  
Membrane Proteins ◽  
Structure Determination ◽  
Cubic Phase ◽  
Technological Advances ◽  
Lipidic Cubic Phase ◽  
High Resolution Structure ◽  
Effects Of Radiation ◽  
G Protein Coupled ◽  
Serial Femtosecond Crystallography

Despite recent technological advances in heterologous expression, stabilization and crystallization of membrane proteins (MPs), their structural studies remain difficult and require new transformative approaches. During the past two years, crystallization in lipidic cubic phase (LCP) has started gaining a widespread acceptance, owing to the spectacular success in high-resolution structure determination of G protein-coupled receptors (GPCRs) and to the introduction of commercial instrumentation, tools and protocols. The recent appearance of X-ray free-electron lasers (XFELs) has enabled structure determination from substantially smaller crystals than previously possible with minimal effects of radiation damage, offering new exciting opportunities in structural biology. The unique properties of LCP material have been exploited to develop special protocols and devices that have established a new method of serial femtosecond crystallography of MPs in LCP (LCP-SFX). In this method, microcrystals are generated in LCP and streamed continuously inside the same media across the intersection with a pulsed XFEL beam at a flow rate that can be adjusted to minimize sample consumption. Pioneering studies that yielded the first room temperature GPCR structures, using a few hundred micrograms of purified protein, validate the LCP-SFX approach and make it attractive for structure determination of difficult-to-crystallize MPs and their complexes with interacting partners. Together with the potential of femtosecond data acquisition to interrogate unstable intermediate functional states of MPs, LCP-SFX holds promise to advance our understanding of this biomedically important class of proteins.

scholarly journals A helical processing pipeline for EM structure determination of membrane proteins

Methods ◽  
2011 ◽  
Vol 55 (4) ◽  
pp. 350-362 ◽  
Author(s):  
Lauren S. Fisher ◽  
Andrew Ward ◽  
Ronald A. Milligan ◽  
Nigel Unwin ◽  
Clinton S. Potter ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Structure Determination ◽  
Processing Pipeline
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