National Magnetic Resonance Facility at Madison (NMRFAM) is a resource that aims to expand the frontiers of biomolecular NMR spectroscopy in solution and the solid state, to ease access for scientists to state-of-the-art spectroscopic methods, and to disseminate technologies broadly to the user community.
NMRFAM provides access to high field (600-900 MHz) solution and solid-state NMR instrumentation and expert staff to assist researchers who would like assistance in experimental design, data acquisition or data analysis. Please contact us with your project ideas and instrumentation needs.
WHAT’S NEW AT NMRFAM
April 27, 2021 – We will have a 15th year (virtual) workshop (May 24-June 11, 2021) based on the 2020 workshop videos. This year’s workshop will provide the 2020 videos along with the recorded live Q&A videos that occurred during that during that workshop. We will have additional live sessions during this year’s workshop to answer any questions that may arise from last year’s video sessions. Send .
Jan, 2021 – Congratulations to NMRFAM! We have secured a 5 years NIH funding titled NMR Technologies for Integrating Structure, Function and Disease. We strive to provide state-of-the-art NMR equipment, technologies and service to assist in NMR solution and solid-state research needs of academic institutions and industries. Read more.
June, 2020 – NMRFAM awarded EAGER grant to study Covid-19!
June 18th, 2020 – Drop-off services on Tuesday and Thursday will start again! Please click here for drop off information.
June 12th, 2020 – UW-Madison Research Restart phase 1 is today! NMRFAM is ramping back up to near- normal operations. External user access via samples shipped to the facility and remote user access have resumed. During Restart phase 1, longer-duration experiments will still be prioritized. Contact NMRFAM staff directly to arrange for other types of experiments.
May 29, 2020: 900 MHz SSNMR! NMRFAM has completed installation of the Phoenix NMR 1.6 mm quadruple resonance probe for HC and HCN modes. Many additional configurations for HFXY, HFX and HXY are available. Example data and more information at Fleckvieh.
May 2020: NMRFAM has partnered with the COVID-19 NMR project to determine protein and RNA structures from SARS-CoV-2 and study the inherent flexibility and dynamics that contribute to the interactions with other proteins and small molecules. Prof. Rienstra is serving on the governing board and Prof. Henzler-Wildman is coordinating the local experimental efforts. Please contact us if you would like to contribute to this project or have questions. See example data so far collected @NMRFAM for NSP7 and NSP8.
April 2020: Welcome Chad Rienstra! Prof. Chad Rienstra joined UW-Madison Biochemistry in January and now is full-time in Madison He and Prof. Katie Henzler-Wildman are now (effective May 17, 2020) co-directors of NMRFAM as Prof. John Markley transitions to emeritus status. As part of Prof. Rienstra’s startup, upgrades are in progress with new magnets, spectrometers and probes customized for magic-angle spinning solid-state NMR spectroscopy applications. Please check the instrumentation page for updates as these capabilities become available to users, and let us know if you would like to request special configurations for your experiments or discuss work plans for your projects.
April 2020: Thank you, John Markley! Prof. John Markley established NMRFAM in 1986. The world class facility that NMRFAM has become is a tribute to his vision and leadership over the past 30+ years. Prof. Markley has made many contributions to the field of NMR and we celebrate his accomplishments and wish him well as he transitions into emeritus status in May.
NMRFAM operates seven solution NMR spectrometers equipped with cryoprobes at fields ranging from 500 to 900 MHz. We offer a range of capabilities, including quadruple resonance cryoprobes with either 31P or 19F in addition to standard 1H, 13C, and 15N. Available pulse sequences and staff expertise span the full range of NMR applications from backbone and side chain assignment, chemical shift perturbation analysis, structure determination, and macromolecular dynamics experiments. NMRFAM staff have developed automated tools for assignment and structure determination of small to mid-sized proteins and have optimized pulse sequences and parameter sets for a wide variety of samples, including large complexes, solubilized membrane proteins and nucleic acids. We are always happy to work with you to implement newly published pulse sequences or adapt experiments for particular samples and applications.
NMRFAM is greatly expanding its solid-state NMR capabilities in 2020, with five spectrometers being installed and upgraded with consoles, amplifiers and magic-angle spinning (MAS) probes. Capabilities already or will soon include 13C-detection at moderate (up to 25 kHz) MAS rates, 1H-detection at MAS rates up to 60 kHz, REDOR (including 31P and 19F), and oriented sample (PISEMA) experiments. Staff are available to support collection of multidimensional data sets at fields ranging from 600 to 900 MHz, as well as support for data analysis and interpretation. NMRFAM is also adding substantial capabilities to study broadband nuclei including quadrupolar nuclei, in support or applications to chemistry, materials science and engineering. Please stay tuned to the NMRFAM SSNMR page for updates as instruments come fully online.
Three of NMRFAM’s spectrometers are equipped with Bruker BioSpin SampleJet sample changers to support data collection for metabolomics, ligand screening and natural products analyses. Metabolomics studies can be performed to identify metabolites and to perform precise quantitation, which is complementary to mass spectrometry-based methods. Ligand screening leverages the existing inventory of metabolites at NMRFAM to perform NMR-based identification of binding interactions (functional assignment of orphan proteins, identification of allosteric interactions or establishing drug leads). Natural products studies by NMR can establish the relative stereochemical configurations through protocols using residual dipolar couplings and force field calculations