title: Crystallization of BMP receptor type IA bound to the antibody Fab fragment AbD1556.
abstract: An antibody Fab fragment, AbD1556, was selected against the extracellular domain of BMP receptor type IA, which blocks the binding of BMP-2 to BMPR-IA and thereby neutralizes BMP-2 activity. To study the mechanism by which BMPR-IA is recognized and bound by the Fab fragment, the complex of AbD1556 bound to BMPR-IA was prepared and crystallized. Crystals of this binary complex belonged to the monoclinic space group P2(1), with unit-cell parameters a=89.32, b=129.25, c=100.24 A, beta=92.27 degrees.
authors.affiliation: Lehrstuhl für Physiologische Chemie II, Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Harth
authors.forename: Alexander
authors.initials: A
authors.lastname: Kotzsch
authors.forename: Walter
authors.initials: W
authors.lastname: Sebald
authors.forename: Thomas Dieter
authors.initials: TD
authors.lastname: Mueller
mesh_terms: D000936:Antigen-Antibody Complex / Q000737:chemistry* / Q000276:immunology; D052005:Bone Morphogenetic Protein Receptors, Type I / Q000737:chemistry* / Q000276:immunology; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry* / Q000276:immunology
chemical_list: D000936:Antigen-Antibody Complex; D007140:Immunoglobulin Fab Fragments; D052005:Bone Morphogenetic Protein Receptors, Type I