FEI, Tsinghua University Announce Structural Biology Research Program
News Feb 05, 2015
FEI and the Tsinghua University Branch of National Center for Protein Sciences Beijing have announced a collaboration to establish a joint new training and research program for cryo-electron microscopy (cryo-EM) in structural biology. With this joint program, the center will feature the first complete cryo-EM workflow in Asia for molecular and cellular structural biologists.
Cryo-EM has achieved a methodological breakthrough to structurally analyze a wide variety of protein complexes at atomic resolution level. This has been a very challenging and nearly impossible task with existing structural technologies, such as crystallography (XRD) and nuclear magnetic resonance (NMR), due to their technical limitations. This largely uncharted field can now be addressed with cryo-EM, and many new researchers will likely be entering the field. The Beijing center’s training and research program will be developed specifically to meet this educational need in Asia.
“The ability to integrate three-dimensional (3D) molecular-scale information from cryo-EM with XRD results as well as NMR data enables researchers to visualize and understand the relationship between structure and function of molecular complexes that may hold the key for central biomedical questions,” states Peter Fruhstorfer, FEI’s vice president and general manager of Life Sciences. “Thus, the boundary conditions are created to gain ground-breaking new insights into the way living systems function, and may lead to promising pathways for the development of effective new medicines and other personalized molecular therapies.”
“We are very enthusiastic about adopting FEI’s workflow solutions into our core facilities,” says Prof. Hongwei Wang, Tsinghua University. “This is a unique opportunity to establish a key collaborative reference site for China and the entire South-East Asia region. The adopted workflow solution opens the door to understanding the structure and function of whole classes of proteins and protein complexes that are simply beyond the capabilities of NMR and XRD alone. An integrative approach that incorporates cryo-EM enables us to begin to look for answers to some of the most important biological questions of our time.”
Prof. Wang adds, “This collaborative effort with FEI to establish a training program at Tsinghua University is a key step in developing the talented and knowledgeable researcher community we need to pursue and maintain leadership in this field.”
Cryo-EM allows researchers to look at large proteins and protein complexes frozen in a near-natural state. In integrative structural biology, EM provides the larger, molecular-scale context for the atomic-scale results of XRD and NMR. FEI’s unique workflow approach addresses all phases of the cryo-EM analytical process, including: sample optimization; cryo-sample preparation; image/data acquisition; image/data analysis; three-dimensional structural modeling; visualization; and presentation.
The workflow is built around FEI’s Titan Krios™, a highly automated, cryo-transmission electron microscope (TEM) designed specifically to meet the needs of structural biologists. In addition to cryo sample handling, the Titan Krios provides the long-term stability and unattended operation required for structural analyses, which may involve hundreds of thousands of images acquired over several days.
The Titan Krios TEM installed at Tsinghua University includes an integrated phase plate, which is a stable, durable solution that increases the contrast of sensitive biological samples and is available on most TEM platforms from FEI.
A CorrSight™ system will also be installed at Tsinghua, which is an advanced light microscope that integrates support of multiple workflows for correlative experiments. It enables quick chemical fixation directly from a live cell imaging experiment for subsequent analysis at the ultra-structural level. In addition, it also allows fluorescence imaging of cryo samples at high resolution to allow for identification of potentially interesting regions in the sample for analysis by cryo-EM.
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