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Improving the diffraction of apoA‐IV crystals through extreme dehydration

Improving the diffraction of apoA‐IV crystals through extreme dehydration Apolipoproteins are the protein component of high‐density lipoproteins (HDL), which are necessary for mobilizing lipid‐like molecules throughout the body. Apolipoproteins undergo self‐association, especially at higher concentrations, making them difficult to crystallize. Here, the crystallization and diffraction of the core fragment of apolipoprotein A‐IV (apoA‐IV), consisting of residues 64–335, is presented. ApoA‐IV64–335 crystallized readily in a variety of hexagonal (P6) morphologies with similar unit‐cell parameters, all containing a long axis of nearly 550 Å in length. Preliminary diffraction experiments with the different crystal morphologies all resulted in limited streaky diffraction to 3.5 Å resolution. Crystal dehydration was applied to the different morphologies with variable success and was also used as a quality indicator of crystal‐growth conditions. The results show that the morphologies that withstood the most extreme dehydration conditions showed the greatest improvement in diffraction. One morphology in particular was able to withstand dehydration in 60% PEG 3350 for over 12 h, which resulted in well defined intensities to 2.7 Å resolution. These results suggest that the approach of integrating dehydration with variation in crystal‐growth conditions might be a general technique to optimize diffraction. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Improving the diffraction of apoA‐IV crystals through extreme dehydration

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References (33)

Publisher
Wiley
Copyright
International Union of Crystallography, 2012
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309111048706
pmid
22232185
Publisher site
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Abstract

Apolipoproteins are the protein component of high‐density lipoproteins (HDL), which are necessary for mobilizing lipid‐like molecules throughout the body. Apolipoproteins undergo self‐association, especially at higher concentrations, making them difficult to crystallize. Here, the crystallization and diffraction of the core fragment of apolipoprotein A‐IV (apoA‐IV), consisting of residues 64–335, is presented. ApoA‐IV64–335 crystallized readily in a variety of hexagonal (P6) morphologies with similar unit‐cell parameters, all containing a long axis of nearly 550 Å in length. Preliminary diffraction experiments with the different crystal morphologies all resulted in limited streaky diffraction to 3.5 Å resolution. Crystal dehydration was applied to the different morphologies with variable success and was also used as a quality indicator of crystal‐growth conditions. The results show that the morphologies that withstood the most extreme dehydration conditions showed the greatest improvement in diffraction. One morphology in particular was able to withstand dehydration in 60% PEG 3350 for over 12 h, which resulted in well defined intensities to 2.7 Å resolution. These results suggest that the approach of integrating dehydration with variation in crystal‐growth conditions might be a general technique to optimize diffraction.

Journal

Acta Crystallographica Section F – Wiley

Published: Jan 1, 2012

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