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Cryo electron microscopy is a collection techniques, including single particle analysis and cryo electron tomography." /> <meta property="og:url" content="https://www.thermofisher.com/blog/atomic-resolution/what-is-cryo-em-what-is-cryo-electron-microscopy/" /> <meta property="og:site_name" content="Life in Atomic Resolution" /> <meta property="article:publisher" content="https://www.facebook.com/thermofisher" /> <meta property="article:published_time" content="2024-10-30T02:00:28+00:00" /> <meta property="article:modified_time" content="2024-10-29T20:08:02+00:00" /> <meta property="og:image" content="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/cryoEM-blog-virus-pore4-1920x600_Header.jpg" /> <meta property="og:image:width" content="1920" /> <meta property="og:image:height" content="600" /> <meta property="og:image:type" content="image/jpeg" /> <meta name="author" content="Alex Ilitchev" /> <meta name="twitter:card" content="summary_large_image" /> <meta name="twitter:creator" content="@thermofisher" /> <meta name="twitter:site" content="@thermofisher" /> <meta name="twitter:label1" content="Written by" /> <meta name="twitter:data1" content="Alex Ilitchev" /> <meta name="twitter:label2" content="Est. reading time" /> <meta name="twitter:data2" content="5 minutes" /> <script type="application/ld+json" class="yoast-schema-graph">{"@context":"https://schema.org","@graph":[{"@type":"WebPage","@id":"https://www.thermofisher.com/blog/atomic-resolution/what-is-cryo-em-what-is-cryo-electron-microscopy/","url":"https://www.thermofisher.com/blog/atomic-resolution/what-is-cryo-em-what-is-cryo-electron-microscopy/","name":"What is Cryo EM? - What is Cryo Electron Microscopy? - Cryo EM Life in Atomic Resolution","isPartOf":{"@id":"https://www.thermofisher.com/blog/atomic-resolution/#website"},"primaryImageOfPage":{"@id":"https://www.thermofisher.com/blog/atomic-resolution/what-is-cryo-em-what-is-cryo-electron-microscopy/#primaryimage"},"image":{"@id":"https://www.thermofisher.com/blog/atomic-resolution/what-is-cryo-em-what-is-cryo-electron-microscopy/#primaryimage"},"thumbnailUrl":"https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/cryoEM-blog-virus-pore4-1920x600_Header.jpg","datePublished":"2024-10-30T02:00:28+00:00","dateModified":"2024-10-29T20:08:02+00:00","author":{"@id":"https://www.thermofisher.com/blog/atomic-resolution/#/schema/person/7b14b1ad2e6aaf9f989f5fb345363e39"},"description":"What is cryo EM? 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}) })(jQuery); </script> </head> <body class="post-template-default single single-post postid-1545 single-format-standard header-image full-width-content genesis-breadcrumbs-visible"><div class="site-container"><header class="site-header"><div class="wrap"><div class="title-area"><p class="site-title"><a href="https://www.thermofisher.com/" title="Thermo Fisher Scientific">Thermo Fisher Scientific</a></p><p class="site-description">Electron and cryo-electron microscopy stories and solutions about the advancement of cellular and structural biology</p></div><div class="widget-area header-widget-area"><section id="block-5" class="widget widget_block"><div class="widget-wrap"> <div class="wp-block-group"><div class="wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow"></div></div> </div></section> <section id="block-6" class="widget widget_block"><div class="widget-wrap"> <div class="wp-block-group"><div class="wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow"></div></div> </div></section> </div><div class="breadcrumb"><span class="breadcrumb-link-wrap"><a href="https://www.thermofisher.com/blog/?">Accelerating Science</a></span><span class="breadcrumb-link-wrap"><a class="breadcrumb-link" href="https://www.thermofisher.com/blog/atomic-resolution/"><span class="breadcrumb-link-text-wrap">Life in Atomic Resolution</span></a><meta ></span> <span aria-label="breadcrumb separator">/</span> <span class="breadcrumb-link-wrap"><a class="breadcrumb-link" href="https://www.thermofisher.com/blog/atomic-resolution/electron-microscopy-101/"><span class="breadcrumb-link-text-wrap">Electron Microscopy 101</span></a><meta ></span> <span aria-label="breadcrumb separator">/</span> <span class="breadcrumb-current-title">What is cryo-EM?</span></div></div></header> <section class="hero-banner" style="background-image:url(https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/cryoEM-blog-virus-pore4-1920x600_Header.jpg)"> </section> <div class="site-inner"><div class="content-sidebar-wrap"><main class="content"><article class="post-1545 post type-post status-publish format-standard has-post-thumbnail category-cryo-em-techniques category-cryo-electron-microscopy-cryo-em category-cryo-electron-tomography category-electron-microscopy-101 category-microed category-single-particle-analysis tag-cryo-em-techniques tag-cryo-em tag-cryo-tomography tag-microcrystal-electron-diffraction tag-single-particle-analysis entry" aria-label="What is cryo-EM?"><header class="entry-header"><h1 class="entry-title">What is cryo-EM?</h1> <span class="post-info-author"> By <a href="https://www.thermofisher.com/blog/author/alexilitchev/" title="Posts by Alex Ilitchev" rel="author">Alex Ilitchev</a> </span> <span class="post-info-date"> 10.30.2024 </span> </header><div class="entry-content"><h2 style="font-size: 100%"><strong>Cryo-EM: cryo electron microscopy</strong></h2> <p>Cryo-electron microscopy (cryo-EM) describes a collection of techniques used to analyze cryogenically frozen samples in specially designed transmission electron microscopes (cryo-TEMs). Recent advancements, including improved sample preparation tools, detectors, and analytical computer algorithms, have even enabled the determination of 3D cryo-EM structures at atomic resolution.</p> <div id="attachment_1546" style="width: 1034px" class="wp-caption aligncenter"><img decoding="async" aria-describedby="caption-attachment-1546" class="size-full wp-image-1546" title="Single particle analysis cryo-EM workflow." src="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-SPA-workflow-1024x170-1.jpg" alt="Single particle analysis cryo-EM workflow." width="1024" height="190" srcset="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-SPA-workflow-1024x170-1.jpg 1024w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-SPA-workflow-1024x170-1-300x56.jpg 300w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-SPA-workflow-1024x170-1-768x143.jpg 768w" sizes="(max-width: 1024px) 100vw, 1024px" /><p id="caption-attachment-1546" class="wp-caption-text">Single particle analysis cryo-EM workflow.</p></div> <h2 style="font-size: 100%"><strong>How does cryo-EM work?</strong></h2> <p>When samples are flash frozen (vitrified), the aqueous solution does not form crystalline ice, instead becoming a vitreous solid. This reduces the damage that the freezing process causes to the sensitive biological sample, thereby taking a “snapshot” of the specimen in solution.</p> <p>Broadly speaking, cryo-EM techniques then image these samples at a variety of angles at high resolution and then digitally recombine the 2D snapshots into a 3D reconstruction. Cryo-EM can determine structures of challenging proteins and other macromolecules while providing wholly unique insights into how these proteins function. Although once considered a specialty tool used only by a small group of experts, cryo-electron microscopes are now increasingly easier to use, more affordable, and accessible to the wider scientific community.</p> <h2 style="font-size: 100%"><strong>Benefits of cryo-EM</strong></h2> <p>Cryo-electron microscopy fills a complimentary niche next to other popular structural analysis techniques such as X-ray diffraction and nuclear magnetic resonance. Compared to other techniques, cryo-EM doesn’t require samples to be crystallized, which has been a significant barrier in the analysis of large complexes and membrane protein. Typically, all that’s required for cryo-EM is that the samples can be suspended in an aqueous environment.</p> <p>Additionally, other techniques that require extensive sample preparation always carry the risk of subtly disrupting the biologically accurate structures as they exist in vivo. Through vitrification, this risk is significantly lowered, thereby providing physiologically relevant observations.</p> <div id="attachment_1547" style="width: 710px" class="wp-caption aligncenter"><img decoding="async" aria-describedby="caption-attachment-1547" class="wp-image-1547" title="Comparison of cryo EM techniques" src="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-comparative-chart-v2.jpg" alt="Comparison of cryo EM techniques" width="700" height="410" srcset="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-comparative-chart-v2.jpg 1024w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-comparative-chart-v2-300x176.jpg 300w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-comparative-chart-v2-768x450.jpg 768w" sizes="(max-width: 700px) 100vw, 700px" /><p id="caption-attachment-1547" class="wp-caption-text">Comparison of common methods for imaging and structural analysis used in the life sciences, including cryo-electron microscopy techniques.</p></div> <h2 style="font-size: 100%"><strong>Cryo-EM techniques</strong></h2> <p>While cryo-EM is sometimes used synonymously with the most popular technique, single particle analysis, there are a suite of analytical methods that can be performed in a cryo-TEM. We will provide a brief introduction to them here; far more information is available on our website.</p> <div id="attachment_1548" style="width: 710px" class="wp-caption aligncenter"><img loading="lazy" decoding="async" aria-describedby="caption-attachment-1548" class="wp-image-1548" title="Histamine in the binding pocket of human GABA-A determined with cryo EM." src="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-SPA-Gabaa-1024x576-1.jpg" alt="Histamine in the binding pocket of human GABA-A determined with cryo EM." width="700" height="394" srcset="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-SPA-Gabaa-1024x576-1.jpg 1024w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-SPA-Gabaa-1024x576-1-300x169.jpg 300w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-SPA-Gabaa-1024x576-1-768x432.jpg 768w" sizes="(max-width: 700px) 100vw, 700px" /><p id="caption-attachment-1548" class="wp-caption-text">Histamine in the binding pocket of human GABA-A (resolved at 1.7 Å with the Krios Cryo-TEM).<br />Data courtesy A. Sente and R. Aricescu, MRC-LMB Cambridge.</p></div> <h2 style="font-size: 100%"><strong>Single particle analysis</strong></h2> <p>In single particle analysis, purified proteins or protein complexes are first vitrified to preserve their native structures. TEM is then used to collect numerous 2D snapshots of the samples. As the proteins are oriented randomly within the ice, these images show the sample at various angles, and can be recombined into a high-resolution 3D reconstruction of the sample.</p> <div id="attachment_1549" style="width: 710px" class="wp-caption aligncenter"><img loading="lazy" decoding="async" aria-describedby="caption-attachment-1549" class="wp-image-1549" title="Cryo-electron tomography visualization of a Golgi apparatus from the green algae Chlamydomonas reinhardtil" src="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-tomo-golgi-1024x626-1.jpg" alt="Cryo-electron tomography visualization of a Golgi apparatus from the green algae Chlamydomonas reinhardtil" width="700" height="428" srcset="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-tomo-golgi-1024x626-1.jpg 1024w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-tomo-golgi-1024x626-1-300x183.jpg 300w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-tomo-golgi-1024x626-1-768x470.jpg 768w" sizes="(max-width: 700px) 100vw, 700px" /><p id="caption-attachment-1549" class="wp-caption-text">Cryo-electron tomography visualization of a Golgi apparatus from the green algae <em>Chlamydomonas reinhardtil</em>.</p></div> <h2 style="font-size: 100%"><strong>Cryo-tomography</strong></h2> <p>Cryo-electron tomography (cryo-ET), most commonly applied to whole cells, provides 3D visualization of organelles and protein complexes at nanometer resolution in their physiological environments. This is done by opening windows into the cell with focused ion beam (FIB) milling of a vitrified cell. A series of 2D images are taken of this thinned cellular sample, which are then reconstructed into a 3D dataset. Such high-resolution 3D images of the cell interior can provide new insights into cellular function and sheds light on the arrangement and structure of native protein complexes.</p> <div id="attachment_1550" style="width: 710px" class="wp-caption aligncenter"><img loading="lazy" decoding="async" aria-describedby="caption-attachment-1550" class="wp-image-1550" title="Protein structure determination with the cryo EM technique microcrystal electron diffraction." src="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-MicroED-1024x568-1.jpg" alt="Protein structure determination with the cryo EM technique microcrystal electron diffraction." width="700" height="388" srcset="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-MicroED-1024x568-1.jpg 1024w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-MicroED-1024x568-1-300x166.jpg 300w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-MicroED-1024x568-1-768x426.jpg 768w, https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2024/10/blog-WhatIsCryoEM-MicroED-1024x568-1-450x250.jpg 450w" sizes="(max-width: 700px) 100vw, 700px" /><p id="caption-attachment-1550" class="wp-caption-text">Protein structure determination with microcrystal electron diffraction.</p></div> <h2 style="font-size: 100%"><strong>Microcrystal electron diffraction</strong></h2> <p>Microcrystal electron diffraction, or MicroED, is a diffraction technique similar to X-ray crystallography (XRD) that utilizes electrons rather than X-rays. Due to electron’s smaller wavelength and stronger interaction with the sample, atomic details can be extracted from individual nanocrystals (<200 nm in size), even in a heterogeneous mixture. This allows for the analysis of crystals that are too small for XRD and other crystallography methods. Data collection is completed in only a few minutes, and 3D structures can be determined at atomic resolution.</p> <h2 style="font-size: 100%"><strong>Conclusions</strong></h2> <p>We hope this brief introduction has given you a glimpse into the power and possibilities of cryo-electron microscopy. With this revolutionary technology, structural biologists can analyze proteins in all their complex conformations, structures, and modified forms. They can even look at multiple protein conformations or heterogeneous complexes in a single sample.</p> <p>If you’d like to know more about cryo-electron microscopy and the ways in which it is revolutionizing structural biology, pharmaceutical research, and more, please see some of our other educational posts on our Life in Atomic Resolution blog:</p> <p>– <a href="https://www.thermofisher.com/blog/atomic-resolution/cryo-em-single-particle-analysis-frequently-asked-questions/">Cryo-EM 101: Frequently Asked Questions</a><br /> – <a href="https://www.thermofisher.com/blog/atomic-resolution/seeing-with-electrons-the-anatomy-of-an-electron-microscope/">Seeing with Electrons: The Anatomy of an Electron Microscope</a><br /> – <a href="https://www.thermofisher.com/blog/atomic-resolution/cellular-cryo-electron-tomography-education/">Open Access: Cellular Cryo-Electron Tomography Education</a><br /> – <a href="https://www.thermofisher.com/blog/atomic-resolution/cryo-em-sample-preparation-a-qa-with-university-of-utahs-core-lab-director/">Cryo-EM Sample Preparation: A Q&A with University of Utah’s Core Lab Director</a></p> <p> </p> <p><strong>For even more educational resources, visit our <a href="https://www.thermofisher.com/us/en/home/electron-microscopy/life-sciences/learning-center.html?cid=msd_ls_xseg_xmkt_xbl_1879311_gl_oso_blg_ownlar&utm_source=comms-blog&utm_medium=blog&utm_campaign=msd_ls_xseg_xmkt_xbl_1879311_gl_oso_blg_ownlar">Life Sciences EM Learning Center >></a></strong></p> <hr /> <p><em>Alex Ilitchev, PhD, is a science writer for Thermo Fisher Scientific.</em></p>  <div class="jp-relatedposts"> <div class="related-post related-1"> <a href="https://www.thermofisher.com/blog/atomic-resolution/finding-new-ways-to-treat-pain-with-novel-opioid-receptor-ligands/"><img width="310" height="274" 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