title: Crystallization and preliminary crystallographic characterization of the N-terminal Kunitz domain of boophilin.
abstract: Boophilin is a tight-binding thrombin inhibitor composed of two canonical Kunitz-type domains in a tandem arrangement. Thrombin-bound boophilin can inhibit a second trypsin-like serine proteinase, most likely through the reactive loop of its N-terminal Kunitz domain. Here, the crystallization and preliminary crystallographic analysis of the isolated N-terminal domain of boophilin is reported. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1) and diffracted to beyond 1.8 Å resolution using a sealed-tube home source and to 0.87 Å resolution at a synchrotron source.
authors.affiliation: IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, 4150-180 Porto, Portugal.
authors.forename: Tatiana B
authors.initials: TB
authors.lastname: Cereija
authors.forename: Ana C
authors.initials: AC
authors.lastname: Figueiredo
authors.forename: Daniele
authors.initials: D
authors.lastname: de Sanctis
authors.forename: Aparecida S
authors.initials: AS
authors.lastname: Tanaka
authors.forename: Pedro José Barbosa
authors.initials: PJ
authors.lastname: Pereira
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010843:Pichia / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013917:Thrombin / Q000037:antagonists & inhibitors
chemical_list: D004791:Enzyme Inhibitors; D005656:Fungal Proteins; D013917:Thrombin