Condensed protein phases play an important role in a wide range of human disorders (eye cataracts, amyotrophic lateral sclerosis, etc.). On the other hand, they are widely used for elucidating protein structures and delivering drugs. Yet, the mechanism of protein crystal formation is unclear. In this paper authors used time-resolved CryoEM to image the process of crystal nucleation. They show that there is no metastable dense liquid phase as the precursor to the crystalline state. In contrast, the nucleation events appeared to be driven by oriented attachments between small crystals.
Structural biology group: science news on web
Saturday, June 30, 2018
Time-resolved CryoEM
Condensed protein phases play an important role in a wide range of human disorders (eye cataracts, amyotrophic lateral sclerosis, etc.). On the other hand, they are widely used for elucidating protein structures and delivering drugs. Yet, the mechanism of protein crystal formation is unclear. In this paper authors used time-resolved CryoEM to image the process of crystal nucleation. They show that there is no metastable dense liquid phase as the precursor to the crystalline state. In contrast, the nucleation events appeared to be driven by oriented attachments between small crystals.
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