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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

Authors :
Brian O. Smith
Alan Riboldi-Tunnicliffe
Marina Ibáñez-Shimabukuro
Andrew J. Roe
Kate Griffiths
Mads Gabrielsen
Malcolm W. Kennedy
Betina Córsico
Alan Cooper
Source :
SEDICI (UNLP), Universidad Nacional de La Plata, instacron:UNLP, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, CONICET Digital (CONICET), Consejo Nacional de Investigaciones Científicas y Técnicas, instacron:CONICET
Publication Year :
2012

Abstract

As-p18, an unusual fatty-acid-binding protein from a parasitic nematode, was expressed in bacteria, purified and crystallized. The use of a microfocus beamline was essential for data collection.<br />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.

Details

Language :
English
ISSN :
17443091
Database :
OpenAIRE
Journal :
SEDICI (UNLP), Universidad Nacional de La Plata, instacron:UNLP, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, CONICET Digital (CONICET), Consejo Nacional de Investigaciones Científicas y Técnicas, instacron:CONICET
Accession number :
edsair.doi.dedup.....2b48f8c67d4d26bf40051b78d2598c34