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  • Title: Solvent organization in the ultrahigh-resolution crystal structure of crambin at room temperature.
    Author: Chen JCH, Gilski M, Chang C, Borek D, Rosenbaum G, Lavens A, Otwinowski Z, Kubicki M, Dauter Z, Jaskolski M, Joachimiak A.
    Journal: IUCrJ; 2024 Sep 01; 11(Pt 5):649-663. PubMed ID: 39190507.
    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.
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