Open AccessUseable diffraction data from a multiple microdomain‐containing crystal of Ascaris suum As‐p18 fatty‐acid‐binding protein using a microfocus beamline
Author(s) -
Gabrielsen Mads,
RiboldiTunnicliffe Alan,
IbáñezShimabukuro Marina,
Griffiths Kate,
Roe Andrew J.,
Cooper Alan,
Smith Brian O.,
Córsico Betina,
Kennedy Malcolm W.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112026553
Subject(s) - ascaris suum , beamline , diffraction , crystallography , fatty acid , fatty acid binding protein , biology , materials science , chemistry , biochemistry , beam (structure) , optics , physics , gene , helminths , zoology
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.