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Updated: Aug 23, 2026

Crystallization of Membrane Proteins in Lipidic Mesophases
Published on: March 28, 2011
Crystallization and initial X-ray analysis of beta-crustacyanin, the dimer of apoproteins A2 and C1, each with a
N E Chayen1, E J Gordon, S E Phillips
1Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, England.
Abstract:
Crystals of beta-crustacyanin, a carotenoid-binding protein from lobster carapace, have been grown under oil from solutions containing sodium potassium phosphate as precipitant. They grow slowly over a period of months to reach maximal dimensions of 0.5 x 0.1 x 0.1 mm, and belong to space group P622 with cell dimensions: a = b = 124.39, c = 188.86 A and gamma = 120 degrees. The crystals diffract to beyond 3 A but are very radiation sensitive, limiting the resolution of usable data. The unit-cell volume suggests that there are two beta-crustacyanin molecules per asymmetric unit.
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