9EWK
Solvent organization in ultrahigh-resolution protein crystal structure at room temperature
Summary for 9EWK
| Entry DOI | 10.2210/pdb9ewk/pdb |
| Descriptor | Crambin, ETHANOL (3 entities in total) |
| Functional Keywords | crambin, plant protein |
| Biological source | Crambe hispanica subsp. abyssinica |
| Total number of polymer chains | 1 |
| Total formula weight | 4820.55 |
| Authors | Chen, J.C.-H.,Gilski, M.,Chang, C.,Borek, D.,Rosenbaum, G.,Lavens, A.,Otwinowski, Z.,Kubicki, M.,Dauter, Z.,Jaskolski, M.,Joachimiak, A. (deposition date: 2024-04-04, release date: 2024-09-04, Last modification date: 2024-11-06) |
| Primary citation | Chen, J.C.H.,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, 11:649-663, 2024 Cited by PubMed 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. PubMed: 39190507DOI: 10.1107/S2052252524007784 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.7 Å) |
Structure validation
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