Our laboratory research program revolves around the themes of new technology development for protein structure production and computational analysis.  Based on our experience as a central node for protein sample production and structure determination by NMR in the NIGMS PSI program, rigorous structure and dynamic analysis of small (< 15 kDa) proteins in our laboratory is largely automated and routine.  However, most of our current research program focus on larger (> 20 kDa), more challenging systems, including integral membrane proteins and protein complexes.  These projects require hybrid approaches, combining NMR data with X-ray crystallography, SAXS, paramagnetic NMR and EPR, and other biophysical methods, along with advanced computational modeling and structural bioinformatics. In order to ensure rigor in applying this broad range of methods, we collaborate intensively with internationally-recognized experts in these domains.  For example, we work with experts to explore the impact of Evolutionary Coupling (C. Sander, D. Marks), Rosetta (D. Baker), and CHARMM (W. Im) modeling methods for determining 3D structures of larger proteins for which only sparse, incomplete experimental data is available, including integral membrane proteins. We also rely on our collaborators in paramagnetic NMR (C. Luchinat and G Parigi), SAXS (J. Tainer), fluorescence spectroscopy (C. Royer), EPR (M. Kennedy), and cryoEM (J. Hunt, K. Das) to provide expertise in these critical experimental methods.  We also lead the structural biology components of several biomedical collaborations, including projects on viral-host protein/RNA interactions of influenza (with S. Patel, Rutgers) and murine leukemia (with M. Roth, Rutgers) viruses, SARS-CoV2 inhibitor development (with A. Garcia-Sastre, Mt. Sinai), DNA damage repair (with S. Bunting, Rutgers), and de novo protein design (with D. Baker, U Wash.).  We also collaborate with the Critical Assessment of Protein Structure Prediction (CASP) program to organize efforts in sparse-NMR-guided structure prediction across the CASP community and AI-based methods for modeling multiple conformations of proteins, and with the wwPDB to develop robust and rigorous methods of protein and nucleic acid structure quality assessment.  All of these collaborations are aimed at ensuring the highest rigor and quality control, and in addressing important biomedical questions.