We offer investigators the latest instrumentation and expertise.
NMR Facility for Biological Research
in the Center for Structural Biology
NMR Facility for Biological Research
About
The NMR Facility for Biological Research operates six NMR spectrometers with proton resonance frequencies from 850 to 500 MHz. Four of the highest field spectrometers (850, 800, 700, 600) are equipped with helium cooled cryoprobes optimized for high-resolution experiments on biological samples in solutions. These high field instruments are dedicated to research projects conducted by laboratories within Center for Structural Biology.
The second 600 MHz spectrometer is set up as reconfigurable development system with multiple probes allowing for high-resolution liquid state as well as biosolids Magic Angle Spinning (MAS) experiments and is sometimes used to perform experiments with special purpose probes.
The Facility operates a fully automated 500 MHz spectrometer designated as an “open access” instrument to all of the FNLCR community. This spectrometer is equipped with broadband X-H/F type nitrogen cooled cryoprobe which is optimized for work on small molecule samples and serves as an analytical tool for a large number of users – particularly from the Chemical Biology Laboratory.
Publications
NMR Selected Recent Publications:
A sampling of recent publications from the NMR Facility is presented below.
2023
Buel, G. R., Chen, X., Myint, W., Kayode, O., Folimonova, V., Cruz, A., Skorupka, K. A., Matsuo, H., Walters, K. J. E6AP AZUL interaction with UBQLN1/2 in cells, condensates, and an AlphaFold-NMR integrated structure. Structure 31(4), 395-410 (2023). doi: https://doi.org/10.1016/j.str.2023.01.012
Buel, G. R., Chen, X., Kayode, O., Cruz, A., and Walters, K. J. 1H, 15N, 13C backbone and Cb resonance assignments for UBQLN1 UBA and UBAA domains. Biomol. NMR assign. (2023) https://doi.org/10.1007/s12104-023-10127-5.
2022
Chen, X.$, Mirazee, J. M. $, Skorupka, K. A., Matsuo, H., Youkharibache, P.*, Taylor, N.*, Walters, K. J.*. The CD8a hinge is intrinsically disordered with a dynamic exchange that includes proline cis-trans isomerization. Journal of Magnetic Resonance (2022) 340:107234. doi: 10.1016/j.jmr.2022.107234. PMID: 35617919 *, co-corresponding author; $, co-first author
Chao, F.A., Dharmaiah, S., Taylor, T., Messing, S., Gillette, W., Esposito, D., Nissley, D.V., McCormick, F., Byrd, R.A., Simanshu, D.K., and Cornilescu, G. (2022). Insights into the Cross Talk between Effector and Allosteric Lobes of KRAS from Methyl Conformational Dynamics. J Am Chem Soc 144, 4196-4205. 10.1021/jacs.2c00007.
2021
Lu, X., Sabbasani, V.R., Osei-Amponsa, V., Evans, C. N., King, J. C., Tarasov, S. G., Dyba, M., Chan, K. C., Schwieters, C. D., Choudhari, S., Fromont, C., Zhao, Y., Tran, B. Chen, X., Matsuo, H. Andresson, T., Chari, R., Swenson, R. E., Tarasova, N. I., and Walters, K. J.: Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13 species upregulated in multiple myeloma, bioRxiv, doi:https://doi.org/10.1101/2021.07.16.452547 (2021); Nat. Commun. (2021) 12:7318 https://doi.org/10.1038/s41467-021-27570-4.
2020
Soubias, O., Pant, S., Heinrich, F., Zhang, Y., Roy, N.S., Li, J., Jian, X., Yohe, M.E., Randazzo, P.A., Losche, M., et al. (2020). Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1. Sci Adv 6. 10.1126/sciadv.abd1882.
2019
Ding, J., Swain, M., Yu, P., Stagno, J. R., Wang, Y. X. Conformational flexibility of adenine riboswitch aptamer in apo and bound states using NMR and an X-ray free electron laser. J. Biomol. NMR., Sep;73(8-9):509-518, 2019. PMID: 31606878 PMCID: PMC6817744
Biancospino, M., Buel, G. R., Niño, C. A., Maspero, E., di Perrotolo, R. S., Raimondi, A., Redlingshöfer, L., Weber, J., Brodsky, F. M.*, Walters, K. J.*, Polo, S.* Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension. Nature Communications, 10(1):4974, 2019. doi: 10.1038/s41467-019-12855-6. *co-corresponding. PMID: 31672988 PMCID: PMC6823378
Chao, F.-A., Li, Y., Zhang, Y., Byrd, R.A. Probing the broad time scale and heterogeneous conformational dynamics in the catalytic core of the Arf-GAP ASAP1 via methyl adiabatic relaxation dispersion. J. Am. Chem. Soc., 141(30):11881-11891, 2019. PMID: 31293161
Solomon, W.C., Myint, W., Hou, S., Kanai, T., Tripathi, R., Yilmaz, N.K., Schiffer, C.A., Matsuo H. Mechanism for APOBEC3G catalytic exclusion of RNA and non-substrate DNA. Nucleic Acids Research, 47(14):7676-7689, 2019. PMID: 31424549 PMCID: PMC6698744
2018
Liu, Y., Holmstrom, E., Yu, P., Tan, K., Zuo, X., Nesbitt, D. J., Sousa, R., Stagno, J. R., Wang, Y. X. Incorporation of isotopic, fluorescent, and heavy-atom-modified nucleotides into RNAs by position-selective labeling of RNA. Nat Protoc., May;13(5):987-1005, 2018. PMID: 29651055
Calabrese, D. R., Chen, X., Leon, E., Gaikwad, S., Phyo, Z., Hewitt, W. M., Alden, S., Hilimire, T. A., He, F., Michalowski, A. M., Simmons, J. K., Saunders, L. B., Zhang, S., Connors, D., Walters, K. J.*, Mock, B. A.*, Schneekloth, J. S. Jr.* Chemical and structural studies provide a mechanistic basis for recognition of the MYC G-quadruplex. Nature Communications, 9:4229, 2018. doi: 10.1038/s41467-018-06315-w. *co-corresponding. PMID: 30315240 PMCID: PMC6185959
Maiti A, Myint W, Kanai T, Delviks-Frankenberry K, Sierra Rodriguez C, Pathak VK, Schiffer CA, Matsuo H. Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA. Nature Communications, Jun 25;9(1):2460, 2018. PMID: 29941968 PMCID: PMC6018426
Contact
Contact Info
Center for Cancer Research National Cancer Institute
- Building 538, Room 187
- Frederick, MD 21702
- 301-846-5213
