Microbiology

Department News

 

Recent high-impact publications

  • Congratulations to Ana Avalos, the 2009 recipient of the Corwin Award, which is given by the Department of Microbiology to a Microbiology graduate student who exemplifies the meaning of outstanding department citizen.
  • The department is happy to announce our 2009 Russek Student Achievement Day award winners:
    Tim Hanley, 1st prize
    Steve Hatch, 2nd prize
  • Faculty Member Wins 2008 Ig Nobel Prize in Chemistry:  Dr. Deborah Anderson was awarded the prestigious Ig Nobel prize for her studies on Coca Cola as a novel form of birth control. Read all about it and the other prize winners at http://improbable.com/ig/winners/#ig2008
  • The department welcomes Dr. Elke Muehlberger, a filovirus expert, who joined the department as an Associate Professor on August 1, 2008.  Dr. Muehlberger came to us from the University of Marburg, Marburg Germany.
  • We would also like to welcome Dr. Katharine Bossart, a Research Associated Professor who is an expert on henipavirus.  Dr. Bossart joined the department on July 1, 2008.  She comes to us from CSIRO Livestock Industries in Geelong, Australia.
  • Click here for a list of previous Microbiology departmental news.

 

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Gly-59, red; Gly-302, green; Pro-306, yellow; Glu-424, cyan. Glutamate binding flap residues Pro-301, Tyr-303, Glu-304, and Ala-305 are colored purple. The amino acid side chains of the Tyr-373 loop (residues 360 to 383) have been removed and its backbone shown as a blue ribbon. The surface exposed alpha-helix (residues 412-431) is shown as an orange ribbon with the side chains omitted. L. Wray, Fisher Laboratory. Space-filling model of Bacillus subtilis glutamine synthetase. The four front subunits are shown in alternating shades of gray while the eight subunits in the back are shaded white. Amino acid residues where substitutions alter the regulation of TnrA and GlnR are colored as follows: Gly-59, red; Gly-302, green; Pro-306, yellow; Glu-424, cyan. Glutamate binding flap residues Pro-301, Tyr-303, Glu-304, and Ala-305 are colored purple. The amino acid side chains of the Tyr-373 loop (residues 360 to 383) have been removed and its backbone shown as a blue ribbon. The surface exposed alpha-helix (residues 412-431) is shown as an orange ribbon with the side chains omitted. L. Wray, Fisher Laboratory.

 

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