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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Clare Peters-LibeuSteven Finkbeiner

Abstract

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 initial crystals gave highly anisotropic diffraction patterns. After optimization of the crystallization conditions and cryoprotectants, a nearly isotropic diffraction pattern at 2.6 A resolution was achieved for crystals with unit-cell parameters a = 133.26, b = 79.52, c = 41.49 A and space group P2(1)2(1)2. Dehydrated crystals diffracted isotropically to 1.9 A with unit-cell parameters a = 123.65, b = 78.25, c = 42.26 A, beta = 90.3 degrees and space group P2(1).

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Citations

Apr 10, 2013·Bioorganic & Medicinal Chemistry·Rafael IschakovEhud Gazit
Jun 3, 2009·Proceedings of the National Academy of Sciences of the United States of America·Yoko Nekooki-MachidaMotomasa Tanaka
Jun 6, 2009·The Journal of Biological Chemistry·Justin LegleiterPaul J Muchowski
Jan 7, 2011·The Journal of Biological Chemistry·Qi Charles ZhangMichelle A Poirier
Mar 22, 2012·The Journal of Biological Chemistry·Leslie G NuciforaMichelle A Poirier
Jan 7, 2011·PloS One·Patrick Lajoie, Erik Lee Snapp
Dec 23, 2009·The Journal of Cell Biology·Leslie Michels ThompsonJoan S Steffan
Feb 7, 2012·Journal of Molecular Biology·Clare Peters-LibeuSteven Finkbeiner
Dec 28, 2011·Experimental Neurology·Montserrat Arrasate, Steven Finkbeiner
Feb 9, 2017·Biochemistry·Adewale AdegbuyiroJustin Legleiter
Apr 24, 2007·Nature Structural & Molecular Biology·Pingwei LiPamela J Bjorkman
Jan 5, 2011·Methods : a Companion to Methods in Enzymology·Hiroshi KubotaKazuhiro Nagata

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