title: Crystallization and preliminary structure determination of an intact human immunoglobulin, b12: an antibody that broadly neutralizes primary isolates of HIV-1.
abstract: An intact human immunoglobulin with a full-length hinge has been crystallized for the first time in a form in which all of the Ig domains are ordered. The IgG1 antibody b12 is one of only three known monoclonal antibodies described that potently neutralize a broad range of HIV-1 primary isolates. It binds to an epitope overlapping the conserved CD4 binding site on the viral surface antigen gp120. Hexagonal crystals corresponding to space group R32 were grown from 0.8 M ammonium sulfate, with unit-cell parameters a = b = 271.3, c = 175.2 A and one molecule per asymmetric unit. The crystals diffract to 2.8 A and a preliminary molecular-replacement solution indicates that all 12 Ig domains of the antibody can be resolved.
authors.affiliation: Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
authors.forename: E O
authors.initials: EO
authors.lastname: Saphire
authors.forename: P W
authors.initials: PW
authors.lastname: Parren
authors.forename: C F
authors.initials: CF
authors.lastname: Barbas
authors.forename: D R
authors.initials: DR
authors.lastname: Burton
authors.forename: I A
authors.initials: IA
authors.lastname: Wilson
mesh_terms: D003460:Crystallization; D015658:HIV Infections / Q000276:immunology; D015497:HIV-1 / Q000276:immunology*; D006801:Humans; D007136:Immunoglobulins / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification; D008297:Male; D009500:Neutralization Tests; D011487:Protein Conformation
chemical_list: D007136:Immunoglobulins