Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen JCH, Gilski M, Chang C, Borek D, Rosenbaum G, Lavens A, Otwinowski Z, Kubicki M, Dauter Z, Jaskolski M, Joachimiak A. Solvent organization in the ultrahigh-resolution crystal structure of crambin at room temperature. IUCrJ. 2024 Sep 1;11(Pt 5):649-663. PMID:39190507 doi:10.1107/S2052252524007784
