Recent News

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Upcoming Presentations: November 2013

Prof. Bush will present the following seminars this November:

  • Department of Chemistry, Pacific Lutheran University, Tacoma, WA, 11/25/13. MFB thanks Prof. Tina Saxowsky for hosting this visit.
  • Joint Chemistry Seminar, Claremont McKenna, Harvey Mudd, Pomona, Pitzer, and Scripps Colleges, Claremont, CA, 11/19/13. MFB thanks the American Society for Mass Spectrometry for travel support and  Prof. Aaron Leconte for hosting this visit.
  • Department of Chemistry & Biochemistry, Northern Illinois University, DeKalb, IL, 11/11/13. MFB thanks Prof. Victor Ryzhov and Prof. Marc Adler for hosting this visit.
  • Department of Chemistry, Mercer University, Macon, GA, 11/1/13. MFB thanks the American Society for Mass Spectrometry for travel support and Prof. Kathryn Kloepper for hosting this visit.
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New Publication: Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity

dn1eThe type II secretion system (T2SS), a multiprotein machinery spanning two membranes in Gram-negative bacteria, is responsible for the secretion of folded proteins from the periplasm across the outer membrane. The critical multidomain T2SS assembly ATPase GspEEpsE had not been structurally characterized as a hexamer. Here, four hexamers of Vibrio cholerae GspEEpsE are obtained when fused to Hcp1 as an assistant hexamer, as shown with native mass spectrometry. The enzymatic activity of the GspEEpsE-Hcp1 fusions is ∼20 times higher than that of a GspEEpsE monomer, indicating that increasing the local concentration of GspEEpsE by the fusion strategy was successful. Crystal structures of GspEEpsE-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspEEpsE with major differences in domain orientation within subunits, and in subunit assembly. SAXS studies on GspEEpsE-Hcp1 fusions suggest that even further variability in GspEEpsE hexamer architecture is likely.

Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity Connie Lu, Stewart Turley, Samuel T. Marionni, Young-Jun Park, Kelly K. Lee, Marcella Patrick, Ripal Shah, Maria Sandkvist, Matthew F. Bush, Wim G.J. Hol. Structure 2013, 21, 1707–1717. (Link|PUBMED)

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Upcoming Presentations: September 2013

Prof. Bush will present the following talks:

  • Native Mass Spectrometry: Ionization, Ion Mobility, and the Mammalian Circadian Clock. Matthew F. Bush. Greater Boston Mass Spectrometry Discussion Group, Boston, MA, 9/19/13. (Additional Information|Flyer)
  • Department of Chemistry & Chemical Biology, Northeastern University, Boston, MA, 9/18/13.
  • Ion mobility mass spectrometry of a mammalian circadian clock protein complex reveals a ligand-dependent conformational switch. Samuel T. Marionni, Weiman Xing, Ning Zheng, Matthew F. Bush. American Chemical Society National Meeting, Indianapolis, IN, 9/11/13. (Additional Information)
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Bush Lab at the 2013 Cascadia Proteomics Symposium

Cascadia Proteomics Symposium

The Bush Lab and collaborators are presenting the following talks at the Cascadia Proteomics Symposium, which takes place at the Institute for Systems Biology in Seattle from July 15-16.

  • Ion Mobility Mass Spectrometry of Native Protein Complex Anions Samuel J. Allen, Alicia M. Schwartz, Matthew F. Bush (Tuesday @ 10:15 AM)
  • Selected Cation to Anion Proton Transfer Kenneth J. Laszlo, Matthew F. Bush (Tuesday @ 10:50 AM)
  • Assembly of the Type II Secretion ATPase Probed by Native Mass Spectrometry Samuel T. Marionni, Connie Lu, Stewart Turley, Young-Jun Park, Kelly Lee, Marcella Patrick, Ripal Shah, Maria Sandkvist, Wim G.J. Hol, Matthew F. Bush (Tuesday @ 1:00 PM)
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Upcoming Presentations: June

  • Prof. Bush will present a talk at the Yale Biological Mass Spectrometry Symposium on June 25th. MFB thanks Prof. Andrew Philips and Suzanne Decatur for organizing this symposium.
  • Prof. Bush will present the University of Minnesota Particle Technology Seminar  on June 20th. MFB thanks Prof. Chris Hogan for hosting this visit.
  • Ion Mobility Mass Spectrometry of Small Molecule, Polymer, and Native Protein Complex Anions Samuel J. Allen; Alicia M. Schwartz; Matthew F. Bush. American Society for Mass Spectrometry Conference. Wednesday, June 12, Poster #737.
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Ion Mobility MS Workshop Program

Ion Mobility Mass Spectrometry: New Instrumentation & Enabling TechnologiesASMS
Matthew F. Bush presiding
Tuesday, June 11th at 5:45 PM | Room 205 AB

The performance of conventional and differential ion mobility mass spectrometers has escalated dramatically in recent years, which can be attributed to improved separations, more efficient ion transfer, and tighter integration of ion mobility devices into hybrid instruments. These improvements enable intricate and sensitive experiments probing mobility selected or separated ions, which has led to the adoption of ion mobility technologies in a wide range of applications, including challenges in gas-phase ion structure determination, native mass spectrometry, proteomics, and systems biology. We will showcase the latest developments in ion mobility mass spectrometry instrumentation and discus remaining challenges.

Prof. Stephen Valentine (West Virginia University)
Miniaturization of Overtone Ion Mobility Spectrometry

Dr. Guillermo Vidal-de-Miguel (SEADM)
Developments in Transversal Modulation IMS (TMIMS): an Add-on enabling absolute IMS-IMS pre-filtration in tandem with MS, and providing 100% DC

Dr. Dimitris Papanastasiou (Fasmatech)
Implementation of a novel Differential Mobility Spectrometry Platform in the Fore Vacuum Region of a Mass Spectrometer

Dr. Melvin Park (Bruker)
High Resolution Trapped Ion Mobility Spectrometry and the Beginnings of a Theory

Dr. Yehia Ibrahim (Pacific Northwest National Laboratory)
The development of the PNNL IMS platform: challenges and solutions