Publications

Acknowledgment and citing the CryoEM Core

Please acknowledge the contributions of our staff and the use of our core facility in your publications.

“We acknowledge Clara Ledger of the UNC CryoEM Core Facility for technical assistance in this project”

“Data was collected at the UNC at Chapel Hill CryoEM Core Facility with a 200 keV Thermo Fisher Scientific Talos Arctica equipped with a Gatan K3 direct electron detector as described.[1]

1. 1. Peck, J.V., J.F. Fay, and J.D. Strauss, High-speed high-resolution data collection on a 200 keV cryo-TEM. IUCrJ, 2022. 9(Pt 2): p. 243-252.

Collaboration Policy

The CryoEM Core’s Collaboration Policy ensures that the intellectual contributions of staff members are recognized. This policy encompasses both routine and non-routine activities, fostering a collaborative environment conducive to scientific advancement.  We follow the guidelines as described by the UNC CH Research Code of Conduct and National Institutes of Health (NIH) General Guidelines for Authorship Contributions.  The CryoEM Core Director Joshua Strauss recognizes that the process of obtaining a structure involves substantial intellectual input beyond technical expertise. Consequently, if a Core staff member is involved in cryoEM data processing or analysis and structure elucidation, it is deemed a collaboration. In such instances, the staff member must be acknowledged as a collaborator in all ensuing publications or presentations.  The determination of whether a Core staff member qualifies as a collaborator aligns with the guidelines established by the NIH. This determination hinges on the extent of their contributions to the project. If a staff member significantly contributes to the conceptualization, design, interpretation of the research project, they will be deemed a collaborator.  This policy extends to encompass non-routine activities, such as the fabrication of TEM grids, the development of novel workflows, sample purification or modification, and advanced 3D image processing and analysis techniques.

List of CryoEM Core publications

2020

1. L. A. Aleksandrov, A. A. Aleksandrov, T. J. Jensen, J. D. Strauss, J. F. Fay, Conformational Variability in Ground-State CFTR Lipoprotein Particle Cryo-EM Ensembles. Int J Mol Sci 23, (2022).
2. B. P. Allen et al., Mapping the Morphological Landscape of Oligomeric Di-block Peptide-Polymer Amphiphiles. Angew Chem Int Ed Engl 61, e202115547 (2022).
3. T. Bepler et al., Smart data collection for CryoEM. J Struct Biol 214, 107913 (2022).
4. G. R. Budziszewski et al., Multivalent DNA and nucleosome acidic patch interactions specify VRK1 mitotic localization and activity. Nucleic Acids Res 50, 4355-4371 (2022).
5. R. H. Gumpper, J. F. Fay, B. L. Roth, Molecular insights into the regulation of constitutive activity by RNA editing of 5HT(2C) serotonin receptors. Cell Rep 40, 111211 (2022).
6. S. Kumar et al., Structural basis of NPR1 in activating plant immunity. Nature 605, 561-566 (2022).
7. C. Lim et al., Drug-Dependent Morphological Transitions in Spherical and Worm-Like Polymeric Micelles Define Stability and Pharmacological Performance of Micellar Drugs. Small 18, e2103552 (2022).
8. Y. Liu et al., Ligand recognition and allosteric modulation of the human MRGPRX1 receptor. Nat Chem Biol, (2022).
9. R. P. McNamara et al., Imaging of surface microdomains on individual extracellular vesicles in 3-D. J Extracell Vesicles 11, e12191 (2022).
10. E. A. Partlow, K. S. Cannon, G. Hollopeter, R. W. Baker, Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Nat Struct Mol Biol 29, 339-347 (2022).
11. J. V. Peck, J. F. Fay, J. D. Strauss, High-speed high-resolution data collection on a 200 keV cryo-TEM. IUCrJ 9, 243-252 (2022).
12. Z. Ren et al., Structural basis for inhibition and regulation of a chitin synthase from Candida albicans. Nat Struct Mol Biol 29, 653-664 (2022).
13. V. Simões et al., Redox-sensitive E2 Rad6 controls cellular response to oxidative stress via K63-linked ubiquitination of ribosomes. Cell Rep 39, 110860 (2022).
14. B. A. Travis et al., Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria. Nat Commun 13, 3793 (2022).
15. Y. Yin et al., Activation mechanism of the mouse cold-sensing TRPM8 channel by cooling agonist and PIP(2). Science 378, eadd1268 (2022).
16. S. Zhang et al., Inactive and active state structures template selective tools for the human 5-HT(5A) receptor. Nat Struct Mol Biol 29, 677-687 (2022).
17. S. Zhang et al., Molecular basis for selective activation of DREADD-based chemogenetics. Nature 612, 354-362 (2022).

2023