Literature DB >> 9541389

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

M Becker1, M T Stubbs, R Huber.   

Abstract

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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Year:  1998        PMID: 9541389      PMCID: PMC2143966          DOI: 10.1002/pro.5560070306

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  14 in total

1.  A genomic clone encoding a cryptophyte phycoerythrin alpha-subunit. Evidence for three alpha-subunits and an N-terminal membrane transit sequence.

Authors:  J Jenkins; R G Hiller; J Speirs; J Godovac-Zimmermann
Journal:  FEBS Lett       Date:  1990-10-29       Impact factor: 4.124

2.  The complete amino-acid sequence and the phylogenetic origin of phycocyanin-645 from the cryptophytan alga Chroomonas sp.

Authors:  W Sidler; H Nutt; B Kumpf; G Frank; F Suter; A Brenzel; W Wehrmeyer; H Zuber
Journal:  Biol Chem Hoppe Seyler       Date:  1990-07

3.  Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A.

Authors:  M Duerring; R Huber; W Bode; R Ruembeli; H Zuber
Journal:  J Mol Biol       Date:  1990-02-05       Impact factor: 5.469

Review 4.  Light guides. Directional energy transfer in a photosynthetic antenna.

Authors:  A N Glazer
Journal:  J Biol Chem       Date:  1989-01-05       Impact factor: 5.157

5.  Crystallographic evidence for the tetrameric subunit structure of L-asparaginase from Escherichia coli.

Authors:  O Epp; W Steigemann; H Formanek; R Huber
Journal:  Eur J Biochem       Date:  1971-06-11

6.  Subunit structure of aldolase: chemical and crystallographic evidence.

Authors:  P A Eagles; L N Johnson; M A Joynson; C H McMurray; H Gutfreund
Journal:  J Mol Biol       Date:  1969-11-14       Impact factor: 5.469

7.  Solvent content of protein crystals.

Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

8.  Determination of the protein content of crystals formed by Mastigocladus laminosus C-phycocyanin, Chroomonas spec. phycocyanin-645 and modified human fibrinogen using an improved Ficoll density gradient method.

Authors:  W Bode; T Schirmer
Journal:  Biol Chem Hoppe Seyler       Date:  1985-03

9.  Molecular topography of the phycocyanin photoreceptor from Chroomonas species.

Authors:  J Jung; P S Song; R J Paxton; M S Edelstein; R Swanson; E E Hazen
Journal:  Biochemistry       Date:  1980-01-08       Impact factor: 3.162

10.  Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 A resolution.

Authors:  K Brejc; R Ficner; R Huber; S Steinbacher
Journal:  J Mol Biol       Date:  1995-06-02       Impact factor: 5.469

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  2 in total

1.  Evolution of a light-harvesting protein by addition of new subunits and rearrangement of conserved elements: crystal structure of a cryptophyte phycoerythrin at 1.63-A resolution.

Authors:  K E Wilk; S J Harrop; L Jankova; D Edler; G Keenan; F Sharples; R G Hiller; P M Curmi
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-03       Impact factor: 11.205

2.  Function-biased choice of additives for optimization of protein crystallization - the case of the putative thioesterase PA5185 from Pseudomonas aeruginosa PAO1.

Authors:  Maksymilian Chruszcz; Matthew D Zimmerman; Shuren Wang; Katarzyna D Koclega; Heping Zheng; Elena Evdokimova; Marina Kudritska; Marcin Cymborowski; Alexei Savchenko; Aled Edwards; Wladek Minor
Journal:  Cryst Growth Des       Date:  2008-11-05       Impact factor: 4.076

  2 in total

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