title: Crystallization and preliminary X-ray diffraction data of mouse L-chain apoferritin crystals.
abstract: Crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique using ammonium sulfate as precipitant. Two crystal forms were observed in the same drop. The crystals belong to either the P2 monoclinic or to the P42(1)2 tetragonal space group. The monoclinic crystals diffracted to beyond 2.4 A resolution but were systematically twinned, while the tetragonal crystals diffracted to beyond 2.9 A. These crystallization conditions in the absence of metal salts should facilitate the study of the interaction between L-chain ferritins and heavy metals, particularly the iron core.
authors.affiliation: Unité de Biophysique Structurale, UMR CNRS 5471, Université Bordeaux I, Bâtiment B8, Avenue des Facultés, 33405 Talence CEDEX, France.
authors.forename: T
authors.initials: T
authors.lastname: Granier
authors.forename: B
authors.initials: B
authors.lastname: Gallois
authors.forename: B
authors.initials: B
authors.lastname: Langlois D'Estaintot
authors.forename: A
authors.initials: A
authors.lastname: Dautant
authors.forename: G
authors.initials: G
authors.lastname: Comberton
authors.forename: J M
authors.initials: JM
authors.lastname: Mellado
authors.forename: C
authors.initials: C
authors.lastname: Beaumont
authors.forename: P
authors.initials: P
authors.lastname: Santambrogio
authors.forename: P
authors.initials: P
authors.lastname: Arosio
authors.forename: G
authors.initials: G
authors.lastname: Precigoux
mesh_terms: D000818:Animals; D001052:Apoferritins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D046911:Macromolecular Substances; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D046911:Macromolecular Substances; D011994:Recombinant Proteins; D001052:Apoferritins