$Crystallization and diffraction properties of the Fab fragment of 3B5H10, an antibody specific for disease-causing polyglutamine stretches$

Crystallization and diffraction properties of the Fab fragment of 3B5H10, an antibody specific for disease-causing polyglutamine stretches

Because it binds soluble forms of proteins with disease‐associated polyglutamine expansions, the antibody 3B5H10 is a powerful tool for studying polyglutamine‐related diseases. Crystals of the 3B5H10 Fab (47 kDa) were obtained by vapor diffusion at room temperature from PEG 3350. However, the initia...

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Veröffentlicht in:	Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-12, Vol.61 (12), p.1065-1068
Hauptverfasser:	Peters-Libeu, Clare, Newhouse, Yvonne, Krishnan, Preethi, Cheung, Kenneth, Brooks, Elizabeth, Weisgraber, Karl, Finkbeiner, Steven
Format:	Artikel
Sprache:	eng
Schlagworte:	3B5H10 ANISOTROPY ANTIBODIES Antibodies - chemistry CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY CRYSTALLIZATION Crystallization Communications Crystallography, X-Ray CRYSTALS DEHYDRATION DIFFRACTION DIFFUSION EXPANSION Fab fragment Humans Huntingtin Protein Immunoglobulin Fragments - chemistry Mutation Nerve Tissue Proteins - chemistry Nuclear Proteins - chemistry OPTIMIZATION Peptides - chemistry Polyethylene Glycols - chemistry polyglutamine expansions PROTEINS RESOLUTION SPACE GROUPS Temperature VAPORS X-Ray Diffraction
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