The Bush Lab is a research group in the Department of Chemistry and the Biological Physics, Structure & Design Program at the University of Washington. Our research focuses on the development and application of mass spectrometry and ion mobility spectrometry techniques to elucidate the structures and assembly of protein complexes and subcellular machines.
- Interested in joining the Bush Lab, click here.
The Bush Lab welcomes Anna Bakhtina, who is an undergraduate biochemistry major. Click here to learn more about Anna.
The Bush Lab welcomes Jack Buckner, who is visiting this summer from Carleton College. Click here to learn more about Jack.
The Bush Lab and collaborators will present the following talks and posters at American Society for Mass Spectrometry Annual Conference in San Antonio, TX (June 5-9):
- Evaluating Gas-Phase Folding of Protein Ions Using Cation to Anion Proton Transfer. Kenneth J. Laszlo; Eleanor B. Munger; Stephanie C. Heard; Matthew F Bush. (MOB 8:50)
- Amino Acid Separation using Different Drift Gases in an RF-Confining Drift Cell. Kimberly Davidson; Matthew F Bush (MOC 9:30)
- Analysis of Native-Like Protein and Protein Complex Ions using Structures for Lossless Ion Manipulations (SLIM). Samuel J. Allen; Rachel M. Eaton; Matthew F. Bush (TP 448)
Sam Allen and Matt Bush will also participate in the Fundamentals Interest Group workshop titled “Modification of Commercial Instruments for Fundamental Research”, which will be held in Room 302A on Tuesday, June 7.
We look forward to seeing everyone in San Antonio!
Congratulations to (from left):
- Sam Allen, who received a graduate student fellowship from the Irving and Mildred Shain Endowed Fund in Chemistry
- Kim Davidson, who received a graduate student fellowship from the Reinhardt Family Endowed Fund in Chemistry
- Rae Eaton, who received a Pacific Northwest National Laboratory Graduate Fellowship and a National Science Foundation Graduate Research Fellowship
- Cece Hong, who received a graduate student fellowship from the Schomaker Endowed Fund in Chemistry
AMS 2017 will be held at the University of Michigan from July 27th to August 1st. We look forward to seeing everyone in Ann Arbor!
Understanding the global biomolecular structure space is an unquestionably important goal for endeavors ranging from the development of new biomaterials to the diagnosis and treatment of human disease. This conference will bring together a wide array of experts that aim to both develop and apply new mass spectrometry (MS) methods in structural biology and biophysics, broadly defined. The timeliness of this conference coincides with the rapidly expanding role of MS in structural biology, which has already made great strides in extracting the details of biomolecule structures from mixtures, using orders of magnitude less sample than other structural probes. Advancing Mass Spectrometry for Biophysics and Structural Biology 2017 will showcase the best science and promote an exchange of ideas between leaders and new-comers to the biology/mass spectrometry interface, in order to propel this exciting topic toward future successes.
The Bush Lab welcomes Meagan Gadzuk-Shea! Click here to learn more about Meagan.
The Bush Lab welcomes Cece Hong! Click here to learn more about Cece.
Prof. Bush will present the following talks this January and February:
- Department of Chemistry, University of Alabama, Tuscaloosa, AL, 2/11/16.
- Department of Chemistry, Florida State University, Tallahassee, FL, 2/4/16.
- Department of Chemistry, University of Florida, Gainesville, FL, 2/3/16.
- Department of Chemistry, University of Oregon, Eugene, OR, 1/25/16.
- Society of Western Analytical Professors (SWAP), University of California, Riverside, CA, 1/29/16.
- Triangle Area Mass Spectrometry Discussion Group, NC, 1/13/16. (Link)
Ion mobility mass spectrometry of peptide, protein, and protein complex ions using a radio-frequency confining drift cell
Samuel J. Allen, Kevin Giles, Tony Gilbert, Matthew F. Bush. Analyst 2016, in press. (Link)
Ion mobility mass spectrometry experiments enable the characterization of mass, assembly, and shape of biological molecules and assemblies. Here, a new radio-frequency confining drift cell is characterized and used to measure the mobilities of peptide, protein, and protein complex ions. The new drift cell replaced the traveling-wave ion mobility cell in a Waters Synapt G2 HDMS. Methods for operating the drift cell and determining collision cross section values using this experimental set up are presented within the context of the original instrument control software. Collision cross sections for 349 cations and anions are reported, 155 of which are for ions that have not been characterized previously using ion mobility. The values for the remaining ions are similar to those determined using a previous radio-frequency confining drift cell and drift tubes without radial confinement. Using this device under 2 Torr of helium gas and an optimized drift voltage, denatured and native-like ions exhibited average apparent resolving powers of 14.2 and 16.5, respectively. For ions with high mobility, which are also low in mass, the apparent resolving power is limited by contributions from ion gating. In contrast, the arrival-time distributions of low-mobility, native-like ions are not well explained using only contributions from ion gating and diffusion. For those species, the widths of arrival-time distributions are most consistent with the presence of multiple structures in the gas phase.