Gabrielsen, M. , Riboldi-Tunnicliffe, A., Ibáñez-Shimabukuro, M., Griffiths, K., Roe, A.J. , Cooper, A., Smith, B. , Córsico, B. and Kennedy, M.W.
(2012)
Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline.
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 68,
pp. 939-941.
(doi: 10.1107/S1744309112026553)
(PMID:22869127)
(PMCID:PMC3412778)
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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 µm.
Item Type: | Articles |
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Status: | Published |
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Refereed: | Yes |
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Glasgow Author(s) Enlighten ID: | Kennedy, Professor Malcolm and Riboldi-Tunnicliffe, Dr Alan and Gabrielsen, Dr Mads and Roe, Professor Andrew and Smith, Dr Brian and Cooper, Professor Alan |
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Authors: |
Gabrielsen, M., Riboldi-Tunnicliffe, A., Ibáñez-Shimabukuro, M., Griffiths, K., Roe, A.J., Cooper, A., Smith, B., Córsico, B., and Kennedy, M.W.
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College/School: | College of Medical Veterinary and Life Sciences > School of Infection & Immunity College of Medical Veterinary and Life Sciences > School of Molecular Biosciences College of Medical Veterinary and Life Sciences > School of Life Sciences College of Science and Engineering > School of Chemistry |
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Journal Name: | Acta Crystallographica. Section F: Structural Biology and Crystallization Communications |
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Publisher: | International Union of Crystallography |
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ISSN: | 1744-3091 |
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ISSN (Online): | 1744-3091 |
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Copyright Holders: | Copyright © 2012 International Union of Crystallography |
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First Published: | First published in Acta Crystallographica. Section F: Structural Biology and Crystallization Communications 68:939-941 |
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Publisher Policy: | Reproduced in accordance with the copyright policy of the publisher |
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