6O2H
Hen lysozyme in triclinic space group at ambient temperature - diffuse scattering dataset
Summary for 6O2H
| Entry DOI | 10.2210/pdb6o2h/pdb |
| Related | 6O2G |
| Descriptor | Lysozyme C, NITRATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | room temperature, diffuse scattering, lysozyme, hydrolase |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 14800.65 |
| Authors | Meisburger, S.P.,Ando, N. (deposition date: 2019-02-22, release date: 2020-02-26, Last modification date: 2024-10-23) |
| Primary citation | Meisburger, S.P.,Case, D.A.,Ando, N. Diffuse X-ray scattering from correlated motions in a protein crystal. Nat Commun, 11:1271-1271, 2020 Cited by PubMed Abstract: Protein dynamics are integral to biological function, yet few techniques are sensitive to collective atomic motions. A long-standing goal of X-ray crystallography has been to combine structural information from Bragg diffraction with dynamic information contained in the diffuse scattering background. However, the origin of macromolecular diffuse scattering has been poorly understood, limiting its applicability. We present a finely sampled diffuse scattering map from triclinic lysozyme with unprecedented accuracy and detail, clearly resolving both the inter- and intramolecular correlations. These correlations are studied theoretically using both all-atom molecular dynamics and simple vibrational models. Although lattice dynamics reproduce most of the diffuse pattern, protein internal dynamics, which include hinge-bending motions, are needed to explain the short-ranged correlations revealed by Patterson analysis. These insights lay the groundwork for animating crystal structures with biochemically relevant motions. PubMed: 32152274DOI: 10.1038/s41467-020-14933-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.212 Å) |
Structure validation
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