Work

Time-resolved structural biology benefits from complementary methods

Year: 2017
Type: article
Abstract: More than 110,500 atomic models based on X-ray crystallography are available in the protein data bank (PDB) and nearly all of them are from diffraction data collected from samples held at 100 K. These cryogenic models provide critical and important functional insights. But, they are snapshots of ground-state molecules or from trapped complexes; whereas biology is dynamic. Indeed, life is governed by the complex interplay within and between macromolecules (proteins, nucleic acids, lipids and carbohydrates) that yield function. Thus, an outstanding frontier challenge in structural biology is to determine time-resolved crystal structures directly from systems engaged in catalysis.
Language: English
Open Access status: bronze
OpenAlex ID: W2778344481
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