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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). 


Effects of Glycans and Hinge on Dynamics in the IgG1 Fc

Christina Bergonzo, J. Todd Hoopes, Zvi Kelman, David Travis Gallagher
The crystallizable fragment (Fc) domain of immunoglobulin subclass IgG1 antibodies is engineered for a wide variety of pharmaceutical applications. Two

Design and characterization of a protein fold switching network

David Travis Gallagher, Biao Ruan, Yanan He, Yingwei Chen, Eun Jung Choi, Yihong Chen, Dana Motabar, Tsega Solomon, Richard Simmerman, Thomas Kauffman, John Orban, Philip Bryan
Protein sequences encoding three common small folds (3-alpha, beta-grasp, and alpha/beta plait) were connected in a network of mutational pathways that

Crystal Structure of a Bivalent Antibody Fab Fragment

Salman Shahid, Mingming Gao, David Travis Gallagher, Steven Foung, Zhen-Yong Keck, Thomas Fuerst, Roy Mariuzza
We determined the crystal structure to 1.8 Å resolution of the Fab fragment of an affinity- matured human monoclonal antibody (HC84.26.5D) that recognizes the
Created October 9, 2019, Updated September 14, 2023