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Search Publications by: David Travis Gallagher (Fed)

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Displaying 26 - 50 of 53

Crystal Structure of the Class IV Adenylyl Cyclase From Yersinia Pestis

March 1, 2006
Author(s)
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
Author(s)
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 1.4.1.1) 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
Author(s)
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
Author(s)
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
Author(s)
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
Author(s)
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
Author(s)
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
Author(s)
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

Chorismate Lyase: Kinetics and Engineering for Stability

January 31, 2002
Author(s)
Marcia J. Holden, M P. Mayhew, David T. Gallagher, V L. Vilker
By removing the enolpyruvyl group from chorismate, chorismate lyase (CL) produces p-hydroxybenzoate (p-HB) for the ubiquinone biosynthetic pathway. We have analyzed CL by several spectroscopic and chemical techniques and measured its kinetic (k cat = 1.7x

The Crystal Structure of Chorismate Lyase Shows a New Fold and a Tightly Retained Product

August 15, 2001
Author(s)
David T. Gallagher, M P. Mayhew, Marcia J. Holden, A J. Howard, K J. Kim, V L. Vilker
The enzyme chorismate lyase (CL) catalyzes the removal of pyruvate from chorismate to produce 4-hydroxy benzoate (4HB) for the ubiquinone pathway. In Escherichia coli, CL is monomeric with 164 residues; we have determined the structure of the CL product

Applying X-Ray Topography and Diffractometry to Improve Protein Crystal Growth

February 21, 2001
Author(s)
David R. Black, L Arnowitz, David T. Gallagher
In order to obtain adequate diffraction data to determine the structure of the protein of interest, crystal quality is important. Although in this context there may be no single concise definition of quality, it must involve adequate size, singleness

Role of Competitive Interactions in Growth Rate Trends of Subtilsin s88 Crystals

May 1, 2000
Author(s)
D Asthagirl, A Lenhoff, David Travis Gallagher
An orthorhombic crystal form of subtilisin BPN' variant s88 exhibits a systematic variation in growth rates of its three unique faces, resulting in pronounced variations in crystal morphology as a function of the ionic strength. We have sought to explain

Crystallization and 1.1 Angstrom Diffraction of Chorismate Lyase From Escherichia Coli

February 1, 2000
Author(s)
C Stover, M P. Mayhew, Marcia J. Holden, A Howard, David Travis Gallagher
Clorismate pathway enzymes are important as producers of nonnucleotide aromatic compounds. The enzyme chorismate layase from Escherichia coli has been crystallized in four distinct forms, three of which have been characterized by x-ray diffraction. Despite

Ultrasonic Measurement of Stress in Pin and Hanger Connections

January 1, 1999
Author(s)
A V. Clark, David T. Gallagher, C S. Hehman, P A. Fuchs, M G. Lozev
Pin and hanger connections are used in bridges to suspend an interior span from the outer spans. The connections can sometimes lock up due to corrosion. If lockup ocurs the stresses in the connection are cycled due to thermal expanison and contraction of