1L2K
Neutron Structure Determination of Sperm Whale Met-Myoglobin at 1.5A Resolution.
Summary for 1L2K
| Entry DOI | 10.2210/pdb1l2k/pdb |
| Descriptor | MYOGLOBIN, SULFATE ION, AMMONIUM CATION WITH D, ... (5 entities in total) |
| Functional Keywords | neutron structure, hydrogen atoms, hydration structure, heme protein, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18065.63 |
| Authors | Ostermann, A.,Tanaka, I.,Engler, N.,Niimura, N.,Parak, F.G. (deposition date: 2002-02-21, release date: 2002-08-21, Last modification date: 2024-04-03) |
| Primary citation | Ostermann, A.,Tanaka, I.,Engler, N.,Niimura, N.,Parak, F.G. Hydrogen and deuterium in myoglobin as seen by a neutron structure determination at 1.5 A resolution. Biophys.Chem., 95:183-193, 2002 Cited by PubMed Abstract: From the first days of protein neutron structure determination sperm whale myoglobin was an object under investigation [Nature 224 (1969) 143, J. Mol. Biol. 220 (1991) 381]. Nevertheless myoglobin is still of interest [Proc. Natl. Acad. Sci. USA 97 (2000) 3872]. The feasibility of the monochromatic neutron diffractometer BIX-3 at the JRR-3M reactor at the JAERI [J. Phys. Chem. Solids 60 (1999) 1623], to collect high-resolution diffraction data in a relatively short time stimulated us to repeat the structural determination of myoglobin. The structure of metmyoglobin has been determined up to a resolution of 1.5 A. The hydrogen atoms were replaced in part, by deuterium soaking the crystals for more than 10 years in D(2)O. A refinement of all atoms has been performed including the refinement of individual mean square displacements and occupancies of the exchangeable protons in backbone hydrogen bonds. A method is described to show clear negative scattering densities of the H atoms. Water molecules within the protein and on the molecule surface are shown. The exchangeability of H atoms is correlated with structural distribution and flexibility. PubMed: 12062378DOI: 10.1016/S0301-4622(01)00255-1 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (1.5 Å) |
Structure validation
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