Mazal H, Wieser FF, Sandoghdar V (2023)
Publication Type: Journal article, Review article
Publication year: 2023
Book Volume: 51
Pages Range: 2041-2059
Journal Issue: 6
DOI: 10.1042/BST20221246
Fluorescence microscopy has witnessed many clever innovations in the last two decades, leading to new methods such as structured illumination and super-resolution microscopies. The attainable resolution in biological samples is, however, ultimately limited by residual motion within the sample or in the microscope setup. Thus, such experiments are typically performed on chemically fixed samples. Cryogenic light microscopy (Cryo-LM) has been investigated as an alternative, drawing on various preservation techniques developed for cryogenic electron microscopy (Cryo-EM). Moreover, this approach offers a powerful platform for correlative microscopy. Another key advantage of Cryo-LM is the strong reduction in photobleaching at low temperatures, facilitating the collection of orders of magnitude more photons from a single fluorophore. This results in much higher localization precision, leading to Angstrom resolution. In this review, we discuss the general development and progress of Cryo-LM with an emphasis on its application in harnessing structural information on proteins and protein complexes. from http://portlandpress.com/biochemsoctrans/article-pdf/51/6/2041/95287
APA:
Mazal, H., Wieser, F.F., & Sandoghdar, V. (2023). Insights into protein structure using cryogenic light microscopy. Biochemical Society Transactions, 51(6), 2041-2059. https://doi.org/10.1042/BST20221246
MLA:
Mazal, Hisham, Franz Ferdinand Wieser, and Vahid Sandoghdar. "Insights into protein structure using cryogenic light microscopy." Biochemical Society Transactions 51.6 (2023): 2041-2059.
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