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Structure of the 30S ribosomal decoding complex at ambient temperature

By E. Han Dao, Frédéric Poitevin, Raymond G. Sierra, Cornelius Gati, Yashas Rao, Halil Ibrahim Ciftci, Fulya Akşit, Alex McGurk, Trevor Obrinski, Paul Mgbam, Brandon Hayes1, Casper De Lichtenberg, Fatima Pardo-Avila, Nicholas Corsepius, Lindsey Zhang, Matthew H. Seaberg, Mark S. Hunter1, Mengling Liang, Jason E. Koglin, Soichi Wakatsuki, Hasan Demirci2

1. SLAC National Accelerator Laboratory 2. Biosciences Division at SLAC National Accelerator Laboratory

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Category

BioXFEL Publications

Published on

Type

journal-article

Author

E. Han Dao and Frédéric Poitevin and Raymond G. Sierra and Cornelius Gati and Yashas Rao and Halil Ibrahim Ciftci and Fulya Akşit and Alex McGurk and Trevor Obrinski and Paul Mgbam and Brandon Hayes and Casper De Lichtenberg and Fatima Pardo-Avila and Nicholas Corsepius and Lindsey Zhang and Matthew H. Seaberg and Mark S. Hunter and Mengling Liang and Jason E. Koglin and Soichi Wakatsuki and Hasan Demirci

Citation

Dao, E.H. et al., 2018. Structure of the 30S ribosomal decoding complex at ambient temperature. RNA, 24(12), pp.1667–1676. Available at: http://dx.doi.org/10.1261/rna.067660.118.

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, 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 to structural studies of RNA and RNA–protein complexes at near-physiological temperatures.

DOI

http://dx.doi.org/10.1261/rna.067660.118