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Search Publications by: David Travis Gallagher (Fed)

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Displaying 26 - 50 of 105

Correction for stray light in optical spectroscopy of crystals

September 1, 2015
Author(s)
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
Author(s)
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

On the need for an international effort to capture, share and use crystallisation screening data (failure and success)

June 1, 2012
Author(s)
David Travis Gallagher, Janet Newman, Evan E. Bolton, Jochen M?Dieckmann, Vincent J. Fazio, David Lovell, Joseph R. Luft, Thomas S. Peat, David Ratcliffe, Roger A. Sayle, Edward H. Snell, Kerry Taylor, Pascal Vallotton, Sameer Velankar, Frank V. Delft
Crystallisation of biological macromolecules is seen by most structural biologists as a necessary evil, a means to the end, which is knowledge about a macromolecular structure. Crystallization remains largely a trial-and-error process, with extensive

The Biological Macromolecule Crystallization Database

March 6, 2012
Author(s)
David Travis Gallagher, Michael Tung
The Biological Macromolecule Crystallization Database (BMCD) is described. The database currently contains 14372 entries with crystallization information for proteins, protein–protein complexes, nucleic acids, nucleic acid–nucleic acid complexes, protein

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

August 5, 2009
Author(s)
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

A New Chemical Reactor for Protein Crystal Growth

October 16, 2008
Author(s)
David Travis Gallagher, C Stover, J Moses, D Charlton, E Steinberg, L Arnowitz
Current rapid advances in the genomic and biochemical sciences provide impetus for finding improved ways of crystallizing proteins for structure determination. A new dialysis-based reactor for protein crystal growth is described. The device utilizes motor

Structure of Archaeal Alanine Dehydrogenase and Relation to Bacterial and Human Proteins

October 16, 2008
Author(s)
David Travis Gallagher, H G. Monbouquette, I Schroeder, Hugh Robinson, Marcia J. Holden, N Smith
In the hyperthermophilic archaeon Archaeoglobus fulgidus, gene AF1665 encodes an L-ala dehydrogenase (AlaDH, EC 1.4.1.1) but has been annotated as an ornithine cyclodeaminase (OCD) based on homology with the mu crystalline/ornithine cyclodeaminase protein