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ISSN: 2161-0398

Journal of Physical Chemistry & Biophysics
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Editorial

High-Resolution Single-Molecule Structure Revealed by Electron Microscopy and Individual Particle Electron Tomography

Lei Zhang and Gang Ren*
The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, USA
Corresponding Author : Gang Ren
The Molecular Foundry
Lawrence Berkeley National Laboratory, Berkeley, USA
Tel: +510- 495-2375
Fax: +510- 486-7268
E-mail: [email protected]
Received May 16, 2012; Accepted May 18, 2012; Published May 22, 2012
Citation: Zhang L, Ren G (2012) High-Resolution Single-Molecule Structure Revealed by Electron Microscopy and Individual-Particle Electron Tomography. J Phys Chem Biophys 2:e103. doi:10.4172/2161-0398.1000e103
Copyright: © 2012 Zhang L, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

The protein is naturally dynamic and heterogeneous in solution. Protein dynamics involves both equilibrium
fluctuations that regulate biological function and other non-equilibrium effects of biological motors, which convert chemical energy to mechanical energy. However, a single, unique structure of protein determined from X-ray crystal and conventional single-particle electron microscopy is insufficient to encompass the dynamic nature of proteins in solution. Structure determination of dynamic and heterogeneous protein is essentially required the determination of each individual particle of protein. Recently, Drs. Gang Ren and Lei Zhan published the first single molecule threedimensional (3D) EM images of individual proteins ever obtained with enough clarity to determine their structure, an IgG antibody (14 Å resolution) and a 17nm HDL (36 Å resolution). These results depended upon four innovations:
i) improved cryo-electron microscopy (cryoEM) sample preparation and Electron microscopy (EM) operation
conditions resulted in the successful imaging of a 17 nm HDL particle (120-200kDa) by cryo-electron tomography (cryoET); ii) developed an optimized NS (OpNS) protocol that eliminates the rouleau artifact that has plagued EM research for three decades. This OpNS protocol provides high-contrast single lipoprotein images with similar size (<5%) and shape (<5%) to that seen by cryoEM; iii) developed a high-resolution and high contrast sample preparation protocol, cryo-positive-staining (cryoPS) that allows direct visualization of the secondary structure of a small protein, such as the β-strands in CETP and the helical double belt of apoA-I in spherical HDL; iv) developed a robust tomography reconstruction method, Individual Particle Electron Tomography (IPET) that is a high-resolution, high throughput reconstruction method that, to the best of our knowledge, is the only method for determining an individual protein structure. Remarkably, IPET went against the conventional wisdom that a single protein can NOT be reconstructed by EM and this opens a door for the study of protein dynamics via a particle-byparticle structural comparison.

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