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The most influential annual technology in 2015: single particle low temperature electron microscopy (cryo-EM).
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The most influential annual technology in 2015: single particle low temperature electron microscopy (cryo-EM). This is a young but potential development for protein three-dimensional structure determination and protein rational design , beyond X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy.
The three-dimensional structure of a protein or protein complex can provide important information about its biological function. For decades, X-ray crystallography has been the preferred method for analysis of protein structure. However, many proteins are difficult to crystallize and achieve membrane protein co-crystallization. Cryo-EM is especially suitable to obtain large protein complexes and displays multiple conformation. Over the past several decades, researchers in this area had made progress steadily, improving resolution of cryo EM and expanding its biocompatibility.
Cryo-EM 3D reconstruction technology, X-ray crystallography and NMR (nuclear magnetic resonance) technology are referred to the three main research methods in structural biology. The main methods for three-dimensional structural analysis by using cryo electron microscopy technique are: single particle analysis method, electron tomography imaging method and electron crystallography.
Although the theoretical system have been established for ten years, but the technology is not developed enough, resolution is not up to standard, and the lowest temperature also can not meet the requirements. Many restrictions hindered the pace of the development of this technology. Only the overall conformation of vague virus can be observed.
In recent years, with the development of physics, enhancement of electron microscopy equipment, and especial application of direct electron detectors in Cryo TEM, cryo-EM 3D reconstruction technique is making an important breakthrough in analyzing the structure of biological macromolecules and their complexes in atomic resolution.
A landmark work is the 3.4 A resolution structure of ion channel membrane protein TRPV1, which plays an important role in pain and thermal perception by cryo-EM single particle analytical method.
The high resolution cryo EM 3D reconstruction bypasses the bottleneck of X-ray crystallography in protein crystallization, which accounts for dominant position in the field of structural biology, opening the door to directly use cryo EM Technology Analysis of membrane proteins and super molecular complex.
Tags: electron microscope, protein, cryo-EM, X-ray crystallography
Source from: http://creative-biostructure.kinja.com/the-rise-of-the-low- temperature-electron-microscope-1785674967?rev=1472009044119.