5B06
Lysozyme (denatured by NaOD and refolded)
Summary for 5B06
| Entry DOI | 10.2210/pdb5b06/pdb |
| Related | 5B05 5B07 |
| Descriptor | Lysozyme C, 1,2-ETHANEDIOL, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | refolded, hydrolase |
| Biological source | Gallus gallus (Chicken) |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 1 |
| Total formula weight | 14905.16 |
| Authors | Kita, A.,Morimoto, Y. (deposition date: 2015-10-28, release date: 2016-01-13, Last modification date: 2024-10-23) |
| Primary citation | Kita, A.,Morimoto, Y. An Effective Deuterium Exchange Method for Neutron Crystal Structure Analysis with Unfolding-Refolding Processes Mol Biotechnol., 58:130-136, 2016 Cited by PubMed Abstract: A method of hydrogen/deuterium (H/D) exchange with an unfolding-refolding process has been applied to hen egg-white lysozyme (HWL), and accurate evaluation of its deuteration was carried out by time-of-flight mass spectroscopy. Neutron crystallography requires a suitable crystal with enough deuterium exchanged in the protein to decrease incoherent scattering from hydrogens. It is very expensive to prepare a fully deuterated protein, and therefore a simple H/D exchange technique is desirable for this purpose. Acid or base addition to protein solutions with heating effectively increased the number of deuterium up to more than 20 % of that of all hydrogen atoms, and refolded structures were determined by X-ray structure analysis at 1.8 Å resolution. Refolded HWL had increased deuterium content in its protein core and its native structure, determined at atomic resolution, was fully preserved. PubMed: 26718545DOI: 10.1007/s12033-015-9908-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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