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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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Crystals of As-p18 obtained using 40% ethylene glycol, 0.1 M acetate pH 4.5.
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fig1: Crystals of As-p18 obtained using 40% ethylene glycol, 0.1 M acetate pH 4.5.

Mentions: Protein crystals appeared within two weeks in condition No. 2 (40% ethylene glycol, 0.1 M acetate pH 4.5) of the Cryo I screen (Emerald BioSystems, USA). The largest crystals had maximum dimensions of 0.08 × 0.08 × 0.1 mm (Fig. 1 ▶). Crystals were cooled without any additional cryoprotection in a stream of gaseous nitrogen cooled to 100 K (Oxford Cryosystems, England) and were stored under liquid nitrogen until diffraction testing.


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)

Crystals of As-p18 obtained using 40% ethylene glycol, 0.1 M acetate pH 4.5.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

fig1: Crystals of As-p18 obtained using 40% ethylene glycol, 0.1 M acetate pH 4.5.
Mentions: Protein crystals appeared within two weeks in condition No. 2 (40% ethylene glycol, 0.1 M acetate pH 4.5) of the Cryo I screen (Emerald BioSystems, USA). The largest crystals had maximum dimensions of 0.08 × 0.08 × 0.1 mm (Fig. 1 ▶). Crystals were cooled without any additional cryoprotection in a stream of gaseous nitrogen cooled to 100 K (Oxford Cryosystems, England) and were stored under liquid nitrogen until diffraction testing.

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