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Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives. | LitMetric

Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives.

Protein Sci

Abteilung für Strukturforschung, Max-Planck-Institut für Biochemie, Martinsried, Germany.

Published: March 1998

Phycoerythrin 545 from the cryptomonad alga, Rhodomonas lens, has been crystallized under a wide variety of conditions. Although this type of photosynthetic light-harvesting protein is water soluble, detergents were always required for crystallization. The crystals were typically poorly ordered, or ordered in only two dimensions. However, crystals that were well-ordered in three dimensions could be obtained under two different conditions. Both used polyethylene glycol as precipitant and the detergent lauryldimethylaminoxide, but the additives that were critical for obtaining well-ordered crystals were propionamide in one case and Cs+/Br- in the other. Crystals obtained in the presence of propionamide have the space group P2(1)2(1)2(1), with cell constants of a = 85.6 angstroms, b = 108.2 angstroms, and c = 131.0 angstroms, and contain two dimers [i.e., 2 x (alpha2beta2)] in the asymmetric unit. They show diffraction to at least 3.0 angstroms resolution. The crystals grown with Cs+/Br- are nearly isomorphous. Both types of crystals show intense, strongly polarized fluorescence, suggesting that energy transfer in the crystals is highly efficient. This should provide a basis for quantitative investigation of the role of exciton interactions in energy transfer in cryptomonad phycobiliproteins.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143966PMC
http://dx.doi.org/10.1002/pro.5560070306DOI Listing

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