In situ serial crystallography facilitates 96-well plate structural analysis at low symmetry.

ABSTRACT: The advent of serial crystallography has rejuvenated and popularized room-temperature X-ray crystal structure determination. Structures determined at physiological temperature reveal protein flexibility and dynamics. In addition, challenging samples (e.g. large complexes, membrane proteins and viruses) form fragile crystals that are often difficult to harvest for cryo-crystallography. Moreover, a typical serial crystallography experiment requires a large number of microcrystals, mainly achievable through batch crystallization. Many medically relevant samples are expressed in mammalian cell lines, producing a meager quantity of protein that is incompatible with batch crystallization. This can limit the scope of serial crystallography approaches. Direct in situ data collection from a 96-well

SUBMITTER: Foos N 

PROVIDER: S-EPMC11364034 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature