title: Crystallization and preliminary X-ray investigation of a recombinant outer membrane protein from Neisseria meningitidis.
abstract: A protein constituent of the outer membrane from Neisseria meningitidis (hereafter called P64K) has been crystallized using the hanging drop technique. Crystals are tetragonal with unit cell dimensions a = b = 136.84 A and c = 78.44 A, compatible with a single monomer of 64 kDa in the asymmetric unit. When exposed to high intensity synchrotron radiation, these crystals diffract X-rays to at least 2.9 A resolution, indicating that a high resolution structure analysis is feasible.
authors.affiliation: CIGB, Cubanacan La Habana, Cuba.
authors.forename: I
authors.initials: I
authors.lastname: Li de la Sierra
authors.forename: T
authors.initials: T
authors.lastname: Prangé
authors.forename: R
authors.initials: R
authors.lastname: Fourme
authors.forename: G
authors.initials: G
authors.lastname: Padrón
authors.forename: P
authors.initials: P
authors.lastname: Fuentes
authors.forename: A
authors.initials: A
authors.lastname: Musacchio
authors.forename: J
authors.initials: J
authors.lastname: Madrazo
mesh_terms: D000942:Antigens, Bacterial / Q000737:chemistry; D001425:Bacterial Outer Membrane Proteins / Q000648:ultrastructure*; D018360:Crystallography, X-Ray; D009345:Neisseria meningitidis / Q000737:chemistry*; D011994:Recombinant Proteins
chemical_list: D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D011994:Recombinant Proteins