Solvent organization in the ultrahigh-resolution crystal structure of crambin at room temperature

Author:

Chen, Julian C H [ORCID]

Gilski, Miroslaw [ORCID]

Chang, Changsoo [ORCID]

Borek, Dominika [ORCID]

Rosenbaum, Gerd [ORCID]

Lavens, Alex

Otwinowski, Zbyszek [ORCID]

Kubicki, Maciej [ORCID]

Dauter, Zbigniew [ORCID]

Jaskolski, Mariusz [ORCID]

Joachimiak, Andrzej [ORCID]
Author Address

Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL 60439, USA., Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan Poland., Department of Biophysics and Department of Biochemistry, The University of Texas Southwestern Medical Center, Dallas, TX USA., Department of Crystallography, Faculty of Chemistry, Adam Mickiewicz University in Poznan, Poznan, Poland., Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA.,

Abstract:

Ultrahigh-resolution structures provide unprecedented details about protein dynamics, hydrogen bonding and solvent networks. The reported 0.70 Å, room-temperature crystal structure of crambin is the highest-resolution ambient-temperature structure of a protein achieved to date. Sufficient data were collected to enable unrestrained refinement of the protein and associated solvent networks using SHELXL. Dynamic solvent networks resulting from alternative side-chain conformations and shifts in water positions are revealed, demonstrating that polypeptide flexibility and formation of clathrate-type structures at hydrophobic surfaces are the key features endowing crambin crystals with extraordinary diffraction power. open access.

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