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

Julian C H ChenMirosław GilskiChangsoo ChangDominika M BorekGerold RosenbaumAlex LavensZbyszek OtwinowskiMaciej KubickiZbigniew DauterMariusz JaskolskiAndrzej Joachimiak
Published in: IUCrJ (2024)
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.
Keyphrases
  • room temperature
  • ionic liquid
  • protein protein
  • single molecule
  • high resolution
  • air pollution
  • solar cells
  • electronic health record
  • cystic fibrosis
  • candida albicans
  • crystal structure