Using cryo-electron microscopy (cryo-EM), Lawrence Berkeley National Laboratory faculty scientist Eva Nogales and her team have made a significant breakthrough in our understanding of how our molecular machinery finds the right DNA to copy, showing with unprecedented detail the role of a powerhouse transcription factor known as TFIID. Read more at the Berkeley Lab News Center.
CRISPR/Cas9: Ready for Action
The CRISPR/Cas9 bacterial genomic editing system identifies and cleaves complementary target sequences in foreign DNA. CRISPR (clustered regularly interspaced short palindromic repeats)–associated (Cas) protein Cas9 begins its work by RNA-guided DNA unwinding to form an RNA-DNA hybrid and displacing a DNA strand inside the protein. Upon binding, Cas9 reorganizes into an R-loop complex that is necessary for it to perform its function. A recent article published in Science describes work done to uncover the structural basis of Cas9’s function.
Single-Particle Cryo-Electron Microscopy Named Method of the Year
Nature Methods recognized the technology for “its newfound ability to determine challenging protein and protein-complex structures at high resolution.” In the journal, the Lab’s Eva Nogales and Robert Glaeser comment on cryo-EM and technological advancements that provide near-atomic resolutions of protein structures without the need for crystallization. The announcement has links to the Nogales and Glaeser Commentaries.
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