TY - JOUR T1 - Structure of the 30S ribosomal decoding complex at ambient temperature JF - bioRxiv DO - 10.1101/262972 SP - 262972 AU - E. Han Dao AU - Frédéric Poitevin AU - Raymond G. Sierra AU - Cornelius Gati AU - Yashas Rao AU - Halil Ibrahim Ciftci AU - Fulya Akşit AU - Alex Mcgurk AU - Trevor Obrinski AU - Paul Mgbam AU - Brandon Hayes AU - Casper De Lichtenberg AU - Fatima Pardo-Avila AU - Nicholas Corsepius AU - Lindsey Zhang AU - Matt Seaberg AU - Mark S. Hunter AU - Mengling Liang AU - Jason E. Koglin AU - Soichi Wakatsuki AU - Hasan Demirci Y1 - 2018/01/01 UR - http://biorxiv.org/content/early/2018/03/09/262972.abstract N2 - 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 lightsources 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, with key residues of the decoding complex exhibiting similar conformations, including adenosine residues 1492 and 1493. Minor variations were observed, namely an alternate conformation of cytosine 1397 near the mRNA channel and the A-site. Our serial crystallography experiment illustrates the amenability of ribosomal microcrystals to routine structural studies at ambient temperature, thus overcoming a long-standing experimental limitation. ER -