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1eyx
From Proteopedia
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'''CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN AT 2.2 ANGSTROMS''' | '''CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN AT 2.2 ANGSTROMS''' | ||
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[[Category: Piras, C.]] | [[Category: Piras, C.]] | ||
[[Category: Vernede, X.]] | [[Category: Vernede, X.]] | ||
| - | [[Category: | + | [[Category: Macroseeding]] |
| - | [[Category: | + | [[Category: Phycobiliprotein]] |
| - | [[Category: | + | [[Category: Protein structure]] |
| - | [[Category: | + | [[Category: R-phycoerythrin]] |
| - | [[Category: | + | [[Category: Red algae]] |
| - | [[Category: | + | [[Category: Sequence]] |
| - | [[Category: | + | [[Category: Twin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:41:15 2008'' | |
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Revision as of 12:41, 2 May 2008
CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN AT 2.2 ANGSTROMS
Overview
R-phycoerythrin, a light-harvesting component from the red algae Gracilaria chilensis, was crystallized by vapour diffusion using ammonium sulfate as precipitant agent. Red crystals grew after one week at 293 K and diffracted to 2.70 A resolution. Three serial macroseeding assays were necessary to grow a second larger crystal to dimensions of 0.68 x 0.16 x 0.16 mm. This crystal diffracted to 2.24 A resolution using synchrotron radiation at beamline BM14 of the European Synchrotron Radiation Facility (ESRF) at Grenoble, France and was used for structure determination. Data were collected at 100 K to a completeness of 98.6%. The crystal was trigonal, space group R3, with unit-cell parameters a = b = 187.3, c = 59.1 A, alpha = beta = 90, gamma = 120 degrees. Data treatment using the CCP4 suite of programs indicated that the crystal was twinned ((I(2))/(I)(2) = 1.41). Molecular replacement was performed with AMoRe using the R-phycoerythrin from Polysiphonia urceolata [Chang et al. (1996), J. Mol. Biol. 249, 424-440] as a search model. In order to overcome the twinning problem, SHELX97 was used for the crystallographic refinement. The twin fraction was 0.48, indicating a nearly perfect hemihedrally twinned crystal. The final R(work) and R(free) factors are 0.16 and 0.25, respectively. All the residues and chromophores of the alpha- and beta-chains are well defined in the electron-density maps. Some residues belonging to the gamma-linker are also recognizable.
About this Structure
1EYX is a Protein complex structure of sequences from Gracilaria chilensis. Full crystallographic information is available from OCA.
Reference
Crystallization and 2.2 A resolution structure of R-phycoerythrin from Gracilaria chilensis: a case of perfect hemihedral twinning., Contreras-Martel C, Martinez-Oyanedel J, Bunster M, Legrand P, Piras C, Vernede X, Fontecilla-Camps JC, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):52-60. PMID:11134927 Page seeded by OCA on Fri May 2 15:41:15 2008
