Structural effects of monovalent anions on polymorphic lysozyme crystals.
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.
Vaney
M C
MC
Laboratoire de Cristallographie et RMN Biologiques, CNRS-UMR 8015, Faculté de Pharmacie, 4 Avenue de l'Observatoire, 75006 Paris, France.
Broutin
I
I
Retailleau
P
P
Douangamath
A
A
Lafont
S
S
Hamiaux
C
C
Prangé
T
T
Ducruix
A
A
Riès-Kautt
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000838:Anions; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation
D000838:Anions; D009113:Muramidase