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Search Publications by

David Travis Gallagher (Fed)

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Displaying 1 - 25 of 46

Structure of the Fc Fragment from the NIST Reference Antibody RM8671

September 1, 2018
David Travis Gallagher, Connor V. Galvin, Ioannis Karageorgos
As the link between antigen binding and immune activation, the antibody Fc region has received extensive structural study. In this report, the structure of the Fc fragment of the NIST IgG1 mAb (reference material 8671) is described at 2.1 Å resolution in

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

December 1, 2017
Darion Spigolon, David Travis 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 are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy

A Bacteriophage Endolysin that Eliminates Intracellular Streptococci

March 15, 2016
Yang Shen, Marilia Barros, Tarek Vennemann, David Travis Gallagher, Yizhou Yin, Sara B. Linden, Ryan D. Heselpoth, Dennis J. Spencer, David M. Donovan, John Moult, Vincent A. Fischetti, Frank Heinrich, Mathias Loesche, Daniel C. Nelson
PlyC, a bacteriophage-encoded A-B endolysin, lyses Streptococcus pyogenes (Spy) on contact and protects mice from upper respiratory Spy colonization. Here, we demonstrate that PlyC is a novel, potent agent for targeting and controlling intracellular Spy

Current and Emerging Technologies to Characterize the Higher-Order Structure of Monoclonal Antibodies

October 15, 2015
John Marino, Robert G. Brinson, Jane E. Ladner, David Travis Gallagher, Luke Arbogast, Richard Huang, Jeffrey W. Hudgens, Elyssia S. Gallagher
In contrast to small molecule therapeutics whose conformations can be absolutely defined by constitution and stereochemistry, biopharmaceuticals are distinguished by the requirement for folding into higher order structures (secondary, tertiary, and

Correction for stray light in optical spectroscopy of crystals

September 1, 2015
Richard W. Hendler, Curtis Meuse, David Travis Gallagher, Joerg Labahn, Jan Kubicek, Paul D. Smith, John W. Kakareka
It has long been known in spectroscopy that light not passing through a sample, but reaching the detector (i.e. stray light) results in a distortion of the spectrum known as absorption- flattening. In spectroscopy with crystals, one must either include

Membrane protein resistance of oligo(ethylene oxide) self-assembled monolayers

July 31, 2014
David J. Vanderah, Marlon L. Walker, David T. Gallagher, Ryan Vierling, Fay Crawshaw
Spectroscopic ellipsometry was used to evaluate the resistance to protein adsorption (RPA) of self- assembled monolayers (SAMs) of HS(CH2)3O(CH2CH2O)6M and [HS(CH2)3CH]2O-(CH2CH2O)6M, where M = CH3 or H, on Au. The SAMs were exposed to fibrinogen, a

Protein crystal engineering of YpAC-IV using a strategy of excess charge reduction

August 5, 2009
David T. Gallagher, N N. Smith, Sung Kim, Howard Robinson, Prasad T. Reddy
The class IV adenylyl cyclase from Yersinia pestis has been engineered to enable crystallization at neutral pH for mechanism studies. The wild-type enzyme crystallized only at pH below 5. Based on the unliganded wild-type structure 2FJT at 1.9 Angstrom

Crystal Structure of the Class IV Adenylyl Cyclase From Yersinia Pestis

March 1, 2006
N Smith, Sung Kim, Prasad T. Reddy, David T. Gallagher
ABSTRACT: The crystal structure of the class IV adenylyl cyclase from Yersinia pestis is reported at 1.9 resolution. The class IV fold is distinct from the previously described folds for class II and class III ACs. The dimeric Yp AC-IV folds into an

Structure of Alanine Dehydrogenase from Archaeoglobus: Active Site Analysis and Relation to Bacterial Cyclodeaminases and Mammalian mu Crystallin

September 3, 2004
David T. Gallagher, H G. Monbouquette, I Schroder, Hugh Robinson, Marcia J. Holden, N Smith
The hyperthermophilic archaeon Archaeoglobus fulgidus contains an L-Ala dehydrogenase (AlaDH, EC that is not homologous to known bacterial dehydrogenases and appears to represent a previously unrecognized archaeal group of NAD-dependent

Local and Global Control Mechanisms in Allosteric Threonine Deaminase

June 1, 2004
David T. Gallagher, D Chinchilla, Herbert Lau, Edward Eisenstein
Allosteric and cooperative control signals were investigated in the tetrameric enzyme threonine deaminase. The tetramer consists of two dimers that associate at the x dyad. The structure pointed the way to use the Q175E mutation to create hybrid tetramers

Crystallization and Phasing of Alanine Dehydrogenase From Archaeoglobus Fulgidus

December 1, 2003
N Smith, M P. Mayhew, Hugh Robinson, A Heroux, D Charlton, Marcia J. Holden, David T. Gallagher
Alanine dehydrogenase (AlaDH) from the hyperthermophilic archaeon A. fudgidus is a dimer of 35 kdal chains. The gene (AF1665) is annotated as an ornithine cyclodeaminase based on homology with the ornithine deaminase/ mu crystallin enzyme family. It

X-Ray Topography of Microgravity-Grown Ribonuclease S Crystals

August 1, 2003
David T. Gallagher, C Stover, D Charlton, L Arnowitz, David R. Black
Crystals of the enzyme RNase S were grown at micro and unit gravity using a dialysis-based dynamically controlled device. Crystals were grown at 24 C on space shuttle flights STS 93 and STS 95. Control crystals were grown simultaneously in ground

Fluorescence Resonance Energy Transfer Between Donor-Acceptor Pair on Two Oligonucleotides Hybridized Adjacently to a DNA Template

January 1, 2003
Lili Wang, Adolfas K. Gaigalas, J L. Blasic, Marcia J. Holden, David T. Gallagher, R Pires
We have used fluorescein as the energy donor and rhodamine as the acceptor to measure the efficiency of fluorescence resonance energy transfer (FRET) in a set of hybridized DNA constructs. The two fluorophores are covalently attached via linkers to two

Structural Basis of Thermostability: Analysis of Stabilizing Mutations in Subtilisin BPN

July 26, 2002
O Almog, David Travis Gallagher, Jane E. Ladner, S Strausberg, Patrick Alexander, Phillip Bryan, G L. Gilliland
The crystal structures of two thermally stabilized subtilisin BPN' variants, S63 and S88, are reported here at 1.8 and 1.9 resolution, respectively. The micromolar affinity calcium-binding site (site A) has been deleted (δ 75-83) in these variants

Synchrotron White-Beam X-Ray Topography of Ribonuclease S Crystals

April 1, 2002
W M. Vetter, David Travis Gallagher, M Dudley
With careful experimental design indexed synchrotron white-beam X-ray topographs of ribonuclease S crystals at ambient temperature could be recorded with a definition and contrast comparable to that of monochromatic beam topographs of other proteins