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Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline.

Gabrielsen M, Riboldi-Tunnicliffe A, Ibáñez-Shimabukuro M, Griffiths K, Roe AJ, Cooper A, Smith BO, Córsico B, Kennedy MW - Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2012)

Bottom Line: 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'.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, Scotland. mgabr@chem.gla.ac.uk

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.

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X-ray diffraction images obtained (a) at station I04 of DLS using the standard beam size of 71.8 × 75 µm and (b) at station MX2 of the Australian Synchrotron using an optimized beam size of 12 × 8 µm.
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fig2: X-ray diffraction images obtained (a) at station I04 of DLS using the standard beam size of 71.8 × 75 µm and (b) at station MX2 of the Australian Synchrotron using an optimized beam size of 12 × 8 µm.

Mentions: Crystals were initially tested at station I04 of Diamond Light Source (DLS), UK with an oscillation of 1° at a wavelength of 0.9763 Å. Although externally the crystals appeared to be well formed, the diffraction spots were diffuse and showed signs of aniosotropy (Fig. 2 ▶a). No indexing could be performed to assign the space group.


Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline.

Gabrielsen M, Riboldi-Tunnicliffe A, Ibáñez-Shimabukuro M, Griffiths K, Roe AJ, Cooper A, Smith BO, Córsico B, Kennedy MW - Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2012)

X-ray diffraction images obtained (a) at station I04 of DLS using the standard beam size of 71.8 × 75 µm and (b) at station MX2 of the Australian Synchrotron using an optimized beam size of 12 × 8 µm.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3412778&req=5

fig2: X-ray diffraction images obtained (a) at station I04 of DLS using the standard beam size of 71.8 × 75 µm and (b) at station MX2 of the Australian Synchrotron using an optimized beam size of 12 × 8 µm.
Mentions: Crystals were initially tested at station I04 of Diamond Light Source (DLS), UK with an oscillation of 1° at a wavelength of 0.9763 Å. Although externally the crystals appeared to be well formed, the diffraction spots were diffuse and showed signs of aniosotropy (Fig. 2 ▶a). No indexing could be performed to assign the space group.

Bottom Line: 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'.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, Scotland. mgabr@chem.gla.ac.uk

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.

Show MeSH