Structure of the 30S ribosomal decoding complex at ambient temperature.
Ontology highlight
ABSTRACT: The ribosome translates nucleotide sequences of messenger RNA to proteins through selection of cognate transfer RNA according to the genetic code. To date, structural studies of ribosomal decoding complexes yielding high-resolution data have predominantly relied on experiments performed at cryogenic temperatures. New light sources like the X-ray free electron laser (XFEL) have enabled data collection from macromolecular crystals at ambient temperature. Here, we report an X-ray crystal structure of the Thermus thermophilus 30S ribosomal subunit decoding complex to 3.45 Å resolution using data obtained at ambient temperature at the Linac Coherent Light Source (LCLS). We find that this ambient-temperature structure is largely consistent with existing cryogenic-temperature crystal structures,
SUBMITTER: Dao EH
PROVIDER: S-EPMC6239188 | biostudies-literature | 2018 Dec
REPOSITORIES: biostudies-literature
ACCESS DATA