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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 8(68), p. 939-941, 2012

DOI: 10.1107/s1744309112026553

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Useable diffraction data from a multiple microdomain-containing crystal ofAscaris suumAs-p18 fatty-acid-binding protein using a microfocus beamline

Journal article published in 2012 by Mads Gabrielsen ORCID, Alan Riboldi-Tunnicliffe ORCID, Marina Ibáñez-Shimabukuro, Kate Griffiths, Andrew J. Roe, Alan Cooper, Brian O. Smith, Betina Córsico, Malcolm W. Kennedy
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Abstract

As-p18 is a fatty-acid-binding protein from the parasitic nematode Ascaris suum. Although it exhibits sequence similarity to mammalian intracellular fatty-acid-binding proteins, it contains features that are unique to nematodes. Crystals were obtained, but initial diffraction data analysis revealed that they were composed of a number of microdomains. Interpretable data could only be collected using a microfocus beamline with a beam size of 12 8 m. © 2012 International Union of Crystallography. All rights reserved.