Welcome to the David H. Russell Research Laboratory at Texas A&M University.

Over the past 20 years the Russell research program has made seminal contributions to developmental IM-MS, and the impact of this work is evidenced by a number of research papers describing instrument development as well as fundamental and applied MALDI and ESI IM-MS. In addition, research in fundamental/developmental mass spectrometry has directly impacted a broad spectrum of applications research. Applications research builds on a growing component of the Russell group research program, i.e., macromolecule and biological mass spectrometry, that was initially focused on addressing questions as to whether structure(s)/conformation(s) of solvent-free gas phase ions can be correlated to solution-phase structures. The research interests have evolved from studies of the structure(s) of small molecule ions to studies of large proteins and protein complexes. These transitions have been made possible by development of new strategies and enabling technologies, most notably a new instrument that combines native ESI with Fourier transform ion mobility spectrometry and Orbitrap mass analyzers. This instrument allows for separation of gas-phase ions on the basis of size-to-charge and mass-to-charge under conditions that allow for 1st-principles determinations of ion-neutral rotationally-averaged collision cross sections. The foray into ion mobility mass spectrometry (IM-MS) initially focused on developing tools for proteomics, both separation strategies and determination of peptide ion structures. The most recently developed IM-MS instrument, a native Fourier-transform-IM-Orbitrap MS that combines advanced drift tube IM systems with high resolution/high m/z range Orbitrap mass analyzers, has opened new vistas for MS-based structural biology. This mass spectrometer, with its unique capabilities, is one of the technology research and development components of an NIH RM1 center, the Native Mass Spectrometry Guided Structural Biology Center, for which Dr. Russell serves as co-PI along with Dr. Vicki Wysocki of Georgia Institute of Technology. Originality/creativity in the Russell research program is further illustrated by the development of a one-of-a-kind cryo-IM-MS instrument, which provided new insights into the effects of hydration on peptide/protein conformational preferences as well as folding/refolding reactions.

Current research is funded by NIH and The Welch Foundation. Our laboratories in the Interdisciplinary Life Sciences Building (ILSB) and the novel MS instruments provide exciting opportunities for collaborative, interdisciplinary research with chemical biologists, biochemists, and other chemists. Novel instrumentation plays an increasingly important role in biological mass spectrometry and the RRG is actively pursuing new instrument methods centered around ion mobility instruments, and focuses on developing more versatile and sensitive methods for structural characterization.