1B2K

Structural effects of monovalent anions on polymorphic lysozyme crystals

Summary for 1B2K

• Entry DOI: 10.2210/pdb1b2k/pdb
• Descriptor: PROTEIN (LYSOZYME), IODIDE ION (3 entities in total)
• Functional Keywords: hydrolase (o-glycosyl), hydrolase
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 2
• Total formula weight: 30819.69

Authors

Vaney, M.C.,Broutin, I.,Ries-Kautt, M.,Ducruix, A. (deposition date: 1998-11-26, release date: 1998-12-02, Last modification date: 2024-11-20)

Primary citation

Vaney, M.C.,Broutin, I.,Retailleau, P.,Douangamath, A.,Lafont, S.,Hamiaux, C.,Prange, T.,Ducruix, A.,Ries-Kautt, M.
Structural effects of monovalent anions on polymorphic lysozyme crystals.
Acta Crystallogr.,Sect.D, 57:929-940, 2001

PubMed Abstract: Understanding direct salt effects on protein crystal polymorphism is addressed by comparing different crystal forms (triclinic, monoclinic, tetragonal and orthorhombic) for hen, turkey, bob white quail and human lysozymes. Four new structures of hen egg-white lysozyme are reported: crystals grown in the presence of NapTS diffracted to 1.85 A, of NaI to 1.6 A, of NaNO(3) to 1.45 A and of KSCN to 1.63 A. These new structures are compared with previously published structures in order to draw a mapping of the surface of different lysozymes interacting with monovalent anions, such as nitrate, chloride, iodide, bromide and thiocyanate. An analysis of the structural sites of these anions in the various lysozyme structures is presented. This study shows common anion sites whatever the crystal form and the chemical nature of anions, while others seem specific to a given geometry and a particular charge environment induced by the crystal packing.

PubMed: 11418760
DOI: 10.1107/S0907444901004504

Experimental method

X-RAY DIFFRACTION (1.6 Å)