@article {47811,
	title = {Highly photostable, reversibly photoswitchable fluorescent protein with high contrast ratio for live-cell superresolution microscopy.},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {113},
	year = {2016},
	month = {2016 Aug 25},
	pages = {10364-9},
	abstract = {<p>Two long-standing problems for superresolution (SR) fluorescence microscopy are high illumination intensity and long acquisition time, which significantly hamper its application for live-cell imaging. Reversibly photoswitchable fluorescent proteins (RSFPs) have made it possible to dramatically lower the illumination intensities in saturated depletion-based SR techniques, such as saturated depletion nonlinear structured illumination microscopy (NL-SIM) and reversible saturable optical fluorescence transition microscopy. The characteristics of RSFPs most critical for SR live-cell imaging include, first, the integrated fluorescence signal across each switching cycle, which depends upon the absorption cross-section, effective quantum yield, and characteristic switching time from the fluorescent "on" to "off" state; second, the fluorescence contrast ratio of on/off states; and third, the photostability under excitation and depletion. Up to now, the RSFPs of the Dronpa and rsEGFP (reversibly switchable EGFP) families have been exploited for SR imaging. However, their limited number of switching cycles, relatively low fluorescence signal, and poor contrast ratio under physiological conditions ultimately restrict their utility in time-lapse live-cell imaging and their ability to reach the desired resolution at a reasonable signal-to-noise ratio. Here, we present a truly monomeric RSFP, Skylan-NS, whose properties are optimized for the recently developed patterned activation NL-SIM, which enables low-intensity (\~{}100 W/cm(2)) live-cell SR imaging at \~{}60-nm resolution at subsecond acquisition times for tens of time points over broad field of view.</p>
},
	issn = {1091-6490},
	doi = {10.1073/pnas.1611038113},
	author = {Zhang, Xi and Zhang, Mingshu and Li, Dong and He, Wenting and Peng, Jianxin and Betzig, Eric and Xu, Pingyong}
}
@article {48135,
	title = {Live cell single molecule-guided Bayesian localization super resolution microscopy.},
	journal = {Cell Research},
	year = {2016},
	month = {2016 Dec 30},
	issn = {1748-7838},
	doi = {10.1038/cr.2015.160},
	author = {Xu, Fan and Zhang, Mingshu and He, Wenting and Han, Renmin and Xue, Fudong and Liu, Zhiyong and Zhang, Fa and Lippincott-Schwartz, Jennifer and Xu, Pingyong}
}
@article {47020,
	title = {Extended-resolution structured illumination imaging of endocytic and cytoskeletal dynamics.},
	journal = {Science (New York, N.Y.)},
	volume = {349},
	year = {2015},
	month = {2015 Aug 28},
	abstract = {<p>Super-resolution fluorescence microscopy is distinct among nanoscale imaging tools in its ability to image protein dynamics in living cells. Structured illumination microscopy (SIM) stands out in this regard because of its high speed and low illumination intensities, but typically offers only a twofold resolution gain. We extended the resolution of live-cell SIM through two approaches: ultrahigh numerical aperture SIM at 84-nanometer lateral resolution for more than 100 multicolor frames, and nonlinear SIM with patterned activation at 45- to 62-nanometer resolution for approximately 20 to 40 frames. We applied these approaches to image dynamics near the plasma membrane of spatially resolved assemblies of clathrin and caveolin, Rab5a in early endosomes, and α-actinin, often in relationship to cortical actin. In addition, we examined mitochondria, actin, and the Golgi apparatus dynamics in three dimensions.</p>
},
	issn = {1095-9203},
	doi = {10.1126/science.aab3500},
	author = {Li, Dong and Shao, Lin and Chen, Bi-Chang and Zhang, Xi and Zhang, Mingshu and Moses, Brian and Milkie, Daniel E and Beach, Jordan R and Hammer, John A and Pasham, Mithun and Kirchhausen, Tomas and Baird, Michelle A and Davidson, Michael W and Xu, Pingyong and Betzig, Eric}
}
