Structural Biology and Cryo-EM Imaging Resources

BER research complementary to the Genomic Science Program

DOE’s Biological and Environmental Research (BER) Program supports structural biology and imaging research via unique crystallography, scattering, spectroscopy, imaging, and cryogenic electron microscopy (cryo-EM) and tomography capabilities available at national neutron and light source user facilities operated by DOE’s Office of Basic Energy Sciences. Cryo-EM is a novel technique that enables characterization of cellular structures and proteins without the need for crystallization.

Structural Biology Techniques Address Sample Diversity. Critical structures and functions in biology occur across a wide range of distances (subnanometers to centimeters) and times (subpicoseconds to minutes). The DOE Office of Biological and Environmental Research makes available a variety of structural biology techniques suited to investigating different sample lengths and experimental time scales. [See bottom of page for image credits.]

BER’s support of user programs at these facilities is designed to provide the scientific community access to world-class experimental tools and scientific and technical expertise in support of their research programs, including areas of BER mission relevance. Facilities are open to users from academia, national laboratories, the private sector, and research institutes. Access is most often obtained through peer-reviewed proposals, with no charge for users who intend to publish their results. For research that is not intended for publication, access is available on a cost-recovery basis.

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Image Credits

Composite image courtesy of Stanford Synchrotron Radiation Lightsource at SLAC National Accelerator Laboratory. Individual images left to right: (1)  Van Stappen, C., et al. 2019. “Spectroscopic Description of the E1 State of Mo Nitrogenase Based on Mo and Fe X-Ray Absorption and Mössbauer Studies,” Inorganic Chemistry 58(18), 12365–376. DOI:10.1021/acs.inorgchem.9b01951. Reprinted under a Creative Commons License (CC BY 4.0). (2) Kim, Y., et al. 2021. “Tipiracil Binds to Uridine Site and Inhibits Nsp15 Endoribonuclease NendoU from SARS-CoV-2,” Communications Biology 4, 193. DOI:10.1038/s42003-021-01735-9. Reprinted under a Creative Commons License (CC BY 4.0). (3) PDB ID: 6MOR. Roh, S. H., et al. 2020. “Cryo-EM and MD Infer Water-Mediated Proton Transport and Autoinhibition Mechanisms of Vo Complex,” Science Advances 6(41), eabb9605. DOI:10.1126/sciadv.abb9605. (4) Courtesy Thomas SpleIstoesser, See also Vandavasi, V. G., et al. 2016. “A Structural Study of CESA1 Catalytic Domain of Arabidopsis Cellulose Synthesis Complex: Evidence for CESA Trimers,” Plant Physiology 170(1), 123–35. DOI:0.1104/pp.15.01356. (5) Reprinted with permission from Roth, M. S., et al. 2017. “Chromosome-Level Genome Assembly and Transcriptome of the Green Alga Chromochloris zofingiensis Illuminates Astaxanthin Production,” Proceedings of the National Academy of Sciences USA 114(21), E4296– 4305. DOI:10.1073/pnas.1619928114. (6) Martin, M. C., et al. 2013. “3D Spectral Imaging with Synchrotron Fourier Transform Infrared Spectro-Microtomography,” Nature Methods 10, 861–64. DOI:10.1038/nmeth.2596. (7) Seyfferth, A. L, et al. 2017. “Evidence for the Root-Uptake of Arsenite at Lateral Root Junctions and Root Apices in Rice (Oryza sativa L.),” Soils 1(1), 3. DOI:10.3390/soils1010003. Reprinted under a Creative Commons License (CC BY 4.0). (8) Courtesy Oak Ridge National Laboratory. See also Dhiman, I., et al. 2017. “Quantifying Root Water Extraction After Drought Recovery Using sub-mm In Situ Empirical Data,” Plant Soil 417, 1–17. DOI:10.1007/s11104-017-3408-5.