Wendy A. Breyer, Ph.D.

Affiliations: 
2001 University of Oregon, Eugene, OR, United States 
Area:
X-ray crystallography, protein folding
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"Wendy Breyer"
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Brian W. Matthews grad student 2001 University of Oregon
 (Structural studies of the processive enzyme, exonuclease I, from Escherichia coli.)
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Publications

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Spatafora G, Corbett J, Cornacchione L, et al. (2015) Interactions of the Metalloregulatory Protein SloR from Streptococcus mutans with Its Metal Ion Effectors and DNA Binding Site. Journal of Bacteriology. 197: 3601-15
Stoll KE, Draper WE, Kliegman JI, et al. (2009) Characterization and structure of the manganese-responsive transcriptional regulator ScaR. Biochemistry. 48: 10308-20
Jameson GB, Anderson BF, Breyer WA, et al. (2002) Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form. Acta Crystallographica. Section D, Biological Crystallography. 58: 955-62
Breyer WA, Matthews BW. (2001) A structural basis for processivity. Protein Science : a Publication of the Protein Society. 10: 1699-711
Breyer WA, Matthews BW. (2000) Structure of Escherichia coli exonuclease I suggests how processivity is achieved. Nature Structural Biology. 7: 1125-8
Quillin ML, Breyer WA, Griswold IJ, et al. (2000) Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme. Journal of Molecular Biology. 302: 955-77
Yang G, Cecconi C, Baase WA, et al. (2000) Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 97: 139-44
Breyer WA, Kingston RL, Anderson BF, et al. (1999) On the molecular-replacement problem in the presence of merohedral twinning: structure of the N-terminal half-molecule of human lactoferrin. Acta Crystallographica. Section D, Biological Crystallography. 55: 129-38
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