9ewk

Solvent organization in ultrahigh-resolution protein crystal structure at room temperature

spinqualitylabelsall models 9ewk, resolution 0.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ewk is a 1 chain structure with sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CRAM_CRAAB The function of this hydrophobic plant seed protein is not known. Publication Abstract from PubMed Ultrahigh-resolution structures provide unprecedented details about protein dynamics, hydrogen bonding and solvent networks. The reported 0.70 A, 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. Solvent organization in the ultrahigh-resolution crystal structure of crambin at room temperature.,Chen JCH, Gilski M, Chang C, Borek D, Rosenbaum G, Lavens A, Otwinowski Z, Kubicki M, Dauter Z, Jaskolski M, Joachimiak A IUCrJ. 2024 Sep 1;11(Pt 5):649-663. doi: 10.1107/S2052252524007784. PMID:39190507 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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