Literature DB >> 15299714

Crystallization and initial X-ray analysis of beta-crustacyanin, the dimer of apoproteins A2 and C1, each with a bound astaxanthin molecule.

N E Chayen1, E J Gordon, S E Phillips, E E Saridakis, P F Zagalsky.   

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.

Entities:  

Year:  1996        PMID: 15299714     DOI: 10.1107/S0907444995015137

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  The molecular basis of the coloration mechanism in lobster shell: beta-crustacyanin at 3.2-A resolution.

Authors:  Michele Cianci; Pierre J Rizkallah; Andrzej Olczak; James Raftery; Naomi E Chayen; Peter F Zagalsky; John R Helliwell
Journal:  Proc Natl Acad Sci U S A       Date:  2002-07-15       Impact factor: 11.205

  1 in total

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