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E. Sethe Burgie

Researcher at University of Wisconsin-Madison

Publications -  18
Citations -  1678

E. Sethe Burgie is an academic researcher from University of Wisconsin-Madison. The author has contributed to research in topics: Bilin & Phytochrome. The author has an hindex of 14, co-authored 16 publications receiving 1325 citations. Previous affiliations of E. Sethe Burgie include Washington University in St. Louis.

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Journal ArticleDOI

Phytochrome B integrates light and temperature signals in Arabidopsis

TL;DR: It is demonstrated that the phytochrome B (phyB) photoreceptor participates in temperature perception through its temperature-dependent reversion from the active Pfr state to the inactive Pr state, and proposed that in addition to its photorecept functions, phyB is a temperature sensor in plants.
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Crystal structure of the photosensing module from a red/far-red light-absorbing plant phytochrome

TL;DR: This 3D structure of the photosensing module (PSM) from a seed plant Phy in the Pr state using the PhyB isoform from Arabidopsis thaliana should enable molecular insights into plant PhY signaling and provide an essential scaffold to redesign their activities for agricultural benefit and as optogenetic reagents.
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Phytochromes: An Atomic Perspective on Photoactivation and Signaling

TL;DR: 3D models reveal complex structural alterations whereby photoisomerization of the bilin drives nanometer-scale movements within the Phy dimer through bilin sliding, hairpin reconfiguration, and spine deformation that ultimately impinge upon the paired signal output domains.
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Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers

TL;DR: A robust way of delivering controlled sample amounts on demand using acoustic droplet ejection coupled with a conveyor belt drive that is optimized for crystallography and spectroscopy measurements of photochemical and chemical reactions over a wide range of time scales is presented.
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Crystal Structure of Deinococcus Phytochrome in the Photoactivated State Reveals a Cascade of Structural Rearrangements during Photoconversion

TL;DR: The structure of the Deinococcus phytochrome photosensory module in its near complete far-red light-absorbing Pfr state is described and the dimeric structure clearly identifies downstream rearrangements that trigger large-scale conformational differences between the dark-adapted and photoactivated states.