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David Travis Gallagher (Fed)

Travis Gallagher studied Electrical Engineering and Computer Science at MIT, and then Biochemistry at the University of Texas (Ph.D. 1990). After an NRC postdoctoral fellowship in protein crystallography with Gary Gilliland, he joined NIST's Biotechnology Division, leading to his present position at NIST/IBBR. He is interested in crystal growth, structure determination, and the functional properties of proteins.

Representative Publications:

"The BMCD database: expanded content and new features", Tung, M & Gallagher, DT, Acta Cryst D65, 18-23 (2009).″ 

"Crystal structure of the class IV adenylyl cyclase reveals a novel fold", Gallagher, DT, Smith, NN, Kim, SK, Heroux, A, Robinson, H & Reddy, PT, J. Mol. Biol. 362, 114-122 (2006).″ 

"Structural analysis of ligand binding and catalysis in CL", Smith, NN, Roitberg, AE, Rivera, E, Howard, A, Holden, MJ, Mayhew, M, Kaistha, S, Gallagher, DT, Archives Biochemistry and Biophysics 445, 72-80 (2006). 

Publications

Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

Author(s)
Darion Spigolon, David T. Gallagher, Adrian Velazquez-Campoy, Donatella Bulone, Jatin Narang, Pier San Biagio, Francesco Cappello, Alberto J. Macario, Everly Conway de Macario, Frank Robb
The human chaperonin complex is a ~ 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we
Created October 9, 2019, Updated June 15, 2021