This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1eyx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1eyx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1eyx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1eyx| PDB=1eyx | SCENE= }}
{{STRUCTURE_1eyx| PDB=1eyx | SCENE= }}
-
'''CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN AT 2.2 ANGSTROMS'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11134927}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11134927 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11134927}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Sequence]]
[[Category: Sequence]]
[[Category: Twin]]
[[Category: Twin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:41:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:13:58 2008''

Revision as of 23:13, 30 June 2008

Template:STRUCTURE 1eyx

CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN AT 2.2 ANGSTROMS

Template:ABSTRACT PUBMED 11134927

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 Tue Jul 1 02:13:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools