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Crystallization and preliminary X-ray diffraction analysis of the red fluorescent protein eqFP611.
Acta Crystallogr D Biol Crystallogr. 2003 Jul; 59(Pt 7):1253-5.AC

Abstract

A novel red fluorescent protein, eqFP611, from the sea anemone Entacmaea quadricolor has been cloned in Escherichia coli. With excitation and emission maxima at 559 and 611 nm, this protein shows the most red-shifted emission and the largest Stokes shift of all non-modified proteins in the green fluorescent protein (GFP) family. The protein fluoresces over a wide pH range (4-10) with high quantum yield (0.45). Its photophysical properties make eqFP611 an excellent marker protein for in vivo labeling in eukaryotic systems as was shown by expression in a mammalian cell culture. eqFP611 has been crystallized in space group P6(5)22, with unit-cell parameters a = b = 77.26, c = 329.49 A. The unit cell contains 12 asymmetric units, with two monomers in each. A molecular-replacement solution has been obtained using the 48.4% homologous red fluorescent protein from Discosoma coral (DsRed).

Authors+Show Affiliations

Department of Biophysics, University of Ulm, 89069 Ulm, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12832776

Citation

Nienhaus, Karin, et al. "Crystallization and Preliminary X-ray Diffraction Analysis of the Red Fluorescent Protein EqFP611." Acta Crystallographica. Section D, Biological Crystallography, vol. 59, no. Pt 7, 2003, pp. 1253-5.
Nienhaus K, Vallone B, Renzi F, et al. Crystallization and preliminary X-ray diffraction analysis of the red fluorescent protein eqFP611. Acta Crystallogr D Biol Crystallogr. 2003;59(Pt 7):1253-5.
Nienhaus, K., Vallone, B., Renzi, F., Wiedenmann, J., & Nienhaus, G. U. (2003). Crystallization and preliminary X-ray diffraction analysis of the red fluorescent protein eqFP611. Acta Crystallographica. Section D, Biological Crystallography, 59(Pt 7), 1253-5.
Nienhaus K, et al. Crystallization and Preliminary X-ray Diffraction Analysis of the Red Fluorescent Protein EqFP611. Acta Crystallogr D Biol Crystallogr. 2003;59(Pt 7):1253-5. PubMed PMID: 12832776.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction analysis of the red fluorescent protein eqFP611. AU - Nienhaus,Karin, AU - Vallone,Beatrice, AU - Renzi,Fabiana, AU - Wiedenmann,Jörg, AU - Nienhaus,G Ulrich, Y1 - 2003/06/27/ PY - 2002/12/23/received PY - 2003/04/17/accepted PY - 2003/7/2/pubmed PY - 2004/3/26/medline PY - 2003/7/2/entrez SP - 1253 EP - 5 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr. D Biol. Crystallogr. VL - 59 IS - Pt 7 N2 - A novel red fluorescent protein, eqFP611, from the sea anemone Entacmaea quadricolor has been cloned in Escherichia coli. With excitation and emission maxima at 559 and 611 nm, this protein shows the most red-shifted emission and the largest Stokes shift of all non-modified proteins in the green fluorescent protein (GFP) family. The protein fluoresces over a wide pH range (4-10) with high quantum yield (0.45). Its photophysical properties make eqFP611 an excellent marker protein for in vivo labeling in eukaryotic systems as was shown by expression in a mammalian cell culture. eqFP611 has been crystallized in space group P6(5)22, with unit-cell parameters a = b = 77.26, c = 329.49 A. The unit cell contains 12 asymmetric units, with two monomers in each. A molecular-replacement solution has been obtained using the 48.4% homologous red fluorescent protein from Discosoma coral (DsRed). SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/12832776/Crystallization_and_preliminary_X_ray_diffraction_analysis_of_the_red_fluorescent_protein_eqFP611_ L2 - http://scripts.iucr.org/cgi-bin/paper?S0907444903008837 DB - PRIME DP - Unbound Medicine ER -