3B6L

Crystal structure of lysozyme folded in SDS and 2-methyl-2,4-pentanediol

Summary for 3B6L

Entry DOI	10.2210/pdb3b6l/pdb
Descriptor	Lysozyme C, DODECYL SULFATE (3 entities in total)
Functional Keywords	egg-white lysozyme, protein-sds complex, mpd, allergen, antimicrobial, bacteriolytic enzyme, glycosidase, hydrolase
Biological source	Gallus gallus (Chicken)
Total number of polymer chains	1
Total formula weight	16524.06
Authors	Michaux, C.,Pouyez, J.,Wouters, J.,Prive, G.G. (deposition date: 2007-10-29, release date: 2008-07-01, Last modification date: 2024-11-06)
Primary citation	Michaux, C.,Pouyez, J.,Wouters, J.,Prive, G.G. Protecting role of cosolvents in protein denaturation by SDS: a structural study. BMC Struct.Biol., 8:29-35, 2008 Cited by PubMed Abstract: Recently, we reported a unique approach to preserve the activity of some proteins in the presence of the denaturing agent, Sodium Dodecyl Sulfate (SDS). This was made possible by addition of the amphipathic solvent 2,4-Methyl-2-PentaneDiol (MPD), used as protecting but also as refolding agent for these proteins. Although the persistence of the protein activity in the SDS/MPD mixture was clearly established, preservation of their structure was only speculative until now. PubMed: 18522744 DOI: 10.1186/1472-6807-8-29 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation