Two-color picosecond time-resolved infrared super-resolution microscopy

Author(s):  
M. Sakai ◽  
T. Ohmori ◽  
M. Fujii
Nano Letters ◽  
2016 ◽  
Vol 16 (7) ◽  
pp. 4062-4068 ◽  
Author(s):  
Xian Hu ◽  
Chaoran Jing ◽  
Xiaochun Xu ◽  
Naotaka Nakazawa ◽  
Virginia W. Cornish ◽  
...  

2019 ◽  
Vol 8 (1) ◽  
Author(s):  
Claudio Bruschini ◽  
Harald Homulle ◽  
Ivan Michel Antolovic ◽  
Samuel Burri ◽  
Edoardo Charbon

Abstract Single-photon avalanche diode (SPAD) arrays are solid-state detectors that offer imaging capabilities at the level of individual photons, with unparalleled photon counting and time-resolved performance. This fascinating technology has progressed at a very fast pace in the past 15 years, since its inception in standard CMOS technology in 2003. A host of architectures have been investigated, ranging from simpler implementations, based solely on off-chip data processing, to progressively “smarter” sensors including on-chip, or even pixel level, time-stamping and processing capabilities. As the technology has matured, a range of biophotonics applications have been explored, including (endoscopic) FLIM, (multibeam multiphoton) FLIM-FRET, SPIM-FCS, super-resolution microscopy, time-resolved Raman spectroscopy, NIROT and PET. We will review some representative sensors and their corresponding applications, including the most relevant challenges faced by chip designers and end-users. Finally, we will provide an outlook on the future of this fascinating technology.


2007 ◽  
Vol 439 (1-3) ◽  
pp. 171-176 ◽  
Author(s):  
Makoto Sakai ◽  
Yasutake Kawashima ◽  
Akihiro Takeda ◽  
Tsutomu Ohmori ◽  
Masaaki Fujii

Acta Naturae ◽  
2017 ◽  
Vol 9 (4) ◽  
pp. 42-51
Author(s):  
S. S. Ryabichko ◽  
◽  
A. N. Ibragimov ◽  
L. A. Lebedeva ◽  
E. N. Kozlov ◽  
...  

2019 ◽  
Author(s):  
Jeffrey Chang ◽  
Matthew Romei ◽  
Steven Boxer

<p>Double-bond photoisomerization in molecules such as the green fluorescent protein (GFP) chromophore can occur either via a volume-demanding one-bond-flip pathway or via a volume-conserving hula-twist pathway. Understanding the factors that determine the pathway of photoisomerization would inform the rational design of photoswitchable GFPs as improved tools for super-resolution microscopy. In this communication, we reveal the photoisomerization pathway of a photoswitchable GFP, rsEGFP2, by solving crystal structures of <i>cis</i> and <i>trans</i> rsEGFP2 containing a monochlorinated chromophore. The position of the chlorine substituent in the <i>trans</i> state breaks the symmetry of the phenolate ring of the chromophore and allows us to distinguish the two pathways. Surprisingly, we find that the pathway depends on the arrangement of protein monomers within the crystal lattice: in a looser packing, the one-bond-flip occurs, whereas in a tighter packing (7% smaller unit cell size), the hula-twist occurs.</p><p> </p><p> </p><p> </p><p> </p><p> </p><p> </p> <p> </p>


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