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The research programs in the Yang lab address at the molecular level how light is detected, perceived, harvested and exploited in biological systems. We develop and apply dynamic crystallography to capture transient structural events at the atomic resolution. Mechanistic understanding of signal transduction in photoreceptors and signaling proteins will lead to bio-inspired synthetic biology strategies for biomedical and renewable energy applications.
We focus on three areas of research: 1) structures and signaling mechanisms of modular photoreceptors; 2) structures and dynamics of light-sensitive systems involved in light harvesting and photosynthesis; 3) methodology development of dynamic crystallography and serial crystallography. We adopt an integrated approach of X-ray crystallography, single-crystal spectroscopy, biochemistry and protein engineering to study the signaling mechanisms of both light-triggered and ligand-triggered systems.
Dynamic crystallography is a powerful tool that enables direction observations of protein structural dynamics at the atomic resolution. Our laboratory is actively pushing this frontier of X-ray crystallography via technical (both hardware and software) innovations. We are committed to promote wide applications of dynamic crystallography via collaborations to study protein dynamics in challenging biological systems.
- Bandara S, Ren Z, Lu L, Zeng X, Shin H, Zhao K-H & Yang X Photoactivation mechanism of a carotenoid-based photoreceptor PNAS 114:6286 doi:10.1073/pnas.1700956114 (2017)
- Zhang F, Ma H, Kwiatkowski D, Bowatte K, Mittmann E, Qasem H, Krauss N, Zeng X, Ren Z, Scheer P, Yang X & Lamparter T Crystal structures of bacterial (6-4) photolyase mutants with impaired DNA repair activity Photochem Photobiol 93:304 doi:10.1111/php.12699 (2017)
- Ren Z, Ren PX, Basulu R & Yang X Transmembrane helices tilt, bend, slide, torque, and unwind between functional states of rhodopsin Sci Rep 6:34129 doi:10.1038/srep34129 (2016)
- Ren Z & Yang X Angular-split/temporal-delay approach to ultrafast protein dynamics at XFELs Acta Cryst D 72:871 doi:10.1107/S2059798316008573 (2016)
- Yang X, Stojković EA, Ozarowski WB, Kuk J, Davydova E & Moffat K Light signaling mechanism of two tandem bacteriophytochromes Structure 23:1179 doi:10.1016/j.str.2015.04.022 (2015)
- Zeng X, Ren Z, Wu Q, Fan J, Peng PP, Tang K, Zhang R, Zhao KH & Yang X Dynamic crystallography reveals early signaling events in ultraviolet photoreceptor UVR8Nature Plants 1:14006, doi:10.1038/nplants.2014.6 (2015)
- Zhou W, Ding WL, Zeng X, Dong LL, Zhao B, Zhou M, Scheer H, Zhao KH & Yang X Structure and mechanism of the phycobiliprotein lyase CpcT J Biol Chem 289:26677, doi:10.1074/jbc.M114.586743 (2014)
- Ren Z, Chan P, Moffat K, Pai EF, Royer WE, Srajer V & Yang X Resolution of structural heterogeneity in dynamic crystallography Acta Cryst D 69:946, doi:10.1107/S0907444913003454 (2013)
- Yang X, Ren Z, Kuk J & Moffat K Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome Nature 479:428, doi:10.1038/nature10506 (2011)
- Yang X, Kuk J & Moffat K Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosabacteriophytochrome PNAS 106:15639, doi:10.1073/pnas.0902178106 (2009)
- Yang X, Kuk J & Moffat K Crystal structure of Pseudomonas aeruginosabacteriophytochrome: photoconversion and signal transduction PNAS 105:14715, doi:10.1073/pnas.0806718105 (2008)
- Yang X, Stojkovic EA, Kuk J & Moffat K Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion PNAS 104:12571, doi:10.1073/pnas.0701737104 (2007)
The University of Chicago, Ph.D., 1995
Northwestern University, Postdoc, 1996-1999