1DPX
STRUCTURE OF HEN EGG-WHITE LYSOZYME
Summary for 1DPX
| Entry DOI | 10.2210/pdb1dpx/pdb |
| Related | 1DPW |
| Descriptor | LYSOZYME, CHLORIDE ION (3 entities in total) |
| Functional Keywords | protein-chloride complex, hydrolase |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 1 |
| Total formula weight | 14402.07 |
| Authors | Weiss, M.S.,Palm, G.J.,Hilgenfeld, R. (deposition date: 1999-12-28, release date: 2000-01-03, Last modification date: 2024-11-20) |
| Primary citation | Weiss, M.S.,Palm, G.J.,Hilgenfeld, R. Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD. Acta Crystallogr.,Sect.D, 56:952-958, 2000 Cited by PubMed Abstract: Hen egg-white lysozyme has been crystallized at slightly alkaline pH using 2-methyl-2,4-pentanediol (MPD) as the precipitant. The crystals are nearly isomorphous to crystals grown at acidic pH using sodium chloride as the precipitant. However, the growth kinetics differ markedly between the two conditions. The major reason for this is a molecule of MPD that binds tightly in between two lysozyme molecules and favors the growth of the crystals along the crystallographic c direction over growth perpendicular to it. PubMed: 10944331DOI: 10.1107/S0907444900006685 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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