Crystallization and preliminary X-ray diffraction analysis of the complex between a human anti-alpha toxin antibody fragment and alpha toxin
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چکیده
منابع مشابه
Crystallization and preliminary X-ray diffraction analysis of the complex between a human anti-interferon antibody fragment and human interferon α-2A
Recombinant human interferon alpha-2A (rhIFN-alpha-2A) has been crystallized in complex with the recombinantly produced Fab fragment of a therapeutic monoclonal antibody (MEDI545; IgG1/kappa) which targets several human interferon alpha subtypes. This constitutes the first reported crystals of a human type I interferon bound to an antibody. The orthorhombic crystals belonged to either space gro...
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MEDI4893 is a neutralizing human monoclonal antibody that targets alpha toxin (AT), and is currently undergoing evaluation in the field of Staphylococcus aureusmediated diseases. We have solved the crystal structure of MEDI4893 Fab bound to monomeric AT at a resolution of 2.56 Å, and further characterized its epitope using various engineered AT variants. We have found that MEDI4893 recognizes a...
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Cholera toxin binds to its ganglioside GM1 receptor via its B-subunit, a pentameric assembly of identical subunits (Mr = 11,600). Diffraction quality crystals of cholera toxin B-subunit have been obtained at room temperature by vapor diffusion with polyethylene glycol in the presence of the nonionic detergent beta-octyl glucoside. The crystals have been characterized with x-radiation as monocli...
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BACKGROUND: Clostridium septicum has played a significant role as a causative agent of many acute fetal diseases in man and animals. Alpha- toxin is the main factor in the pathogenesis of C. septicum with hemolytic, necrotic and lethal activities. OBJECTIVES: The study was designed to evaluate alpha-toxin purification and antibody production rate against a local strain of C. septicum NH2 which ...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2013
ISSN: 1744-3091
DOI: 10.1107/s1744309113002881