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Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar.
Acta Crystallogr D Biol Crystallogr. 2002 Sep; 58(Pt 9):1501-3.AC

Abstract

Two variants (wild type and V152C mutant) of a bifunctional poplar peroxiredoxin have been overexpressed in Escherichia coli cells. The two recombinant enzymes were purified and crystallized using the hanging-drop vapour-diffusion technique. Data sets were collected to 1.62 and 2.48 A resolution using X-ray synchrotron-source radiation from two crystal forms of wild-type peroxiredoxin which belonged to the monoclinic space group P2(1) (with unit-cell parameters a = 59.26, b = 68.80, c = 75.71 A, beta = 93.45 degrees) and to the orthorhombic space group P2(1)2(1)2 (with unit-cell parameters a = 64.70, b = 130.73, c = 35.59 A), respectively. Data were also collected to 2.17 A resolution using a home X-ray source from a V152C peroxiredoxin crystal which belongs to the triclinic space group (P1), with unit-cell parameters a = 36.65, b = 41.53, c = 58.06 A, alpha = 70.52, beta = 93.45, gamma = 64.31 degrees. Phases have been obtained using molecular replacement with the structure of human peroxiredoxin V (PDB code 1hd2) as a search model. Refinement of the structures is in progress.

Authors+Show Affiliations

Echalier A
LCM3B, Groupe Biocristallographie, UMR 7036, UHP, Faculté des Sciences, 54506 Vandoeuvre CEDEX, France.
Corbier C
No affiliation info available
Rouhier N
No affiliation info available
Jacquot JP
No affiliation info available
Aubry A
No affiliation info available

MeSH

Cloning, MolecularCrystallizationCrystallography, X-RayPeroxidasesPeroxiredoxinsProtein ConformationRecombinant ProteinsTrees

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12198315

Citation

Echalier, Aude, et al. "Crystallization and Preliminary X-ray Data of a Bifunctional Peroxiredoxin From Poplar." Acta Crystallographica. Section D, Biological Crystallography, vol. 58, no. Pt 9, 2002, pp. 1501-3.
Echalier A, Corbier C, Rouhier N, et al. Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar. Acta Crystallogr D Biol Crystallogr. 2002;58(Pt 9):1501-3.
Echalier, A., Corbier, C., Rouhier, N., Jacquot, J. P., & Aubry, A. (2002). Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar. Acta Crystallographica. Section D, Biological Crystallography, 58(Pt 9), 1501-3.
Echalier A, et al. Crystallization and Preliminary X-ray Data of a Bifunctional Peroxiredoxin From Poplar. Acta Crystallogr D Biol Crystallogr. 2002;58(Pt 9):1501-3. PubMed PMID: 12198315.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray data of a bifunctional peroxiredoxin from poplar. AU - Echalier,Aude, AU - Corbier,Catherine, AU - Rouhier,Nicolas, AU - Jacquot,Jean Pierre, AU - Aubry,André, Y1 - 2002/08/23/ PY - 2002/04/11/received PY - 2002/07/03/accepted PY - 2002/8/29/pubmed PY - 2003/2/14/medline PY - 2002/8/29/entrez SP - 1501 EP - 3 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 58 IS - Pt 9 N2 - Two variants (wild type and V152C mutant) of a bifunctional poplar peroxiredoxin have been overexpressed in Escherichia coli cells. The two recombinant enzymes were purified and crystallized using the hanging-drop vapour-diffusion technique. Data sets were collected to 1.62 and 2.48 A resolution using X-ray synchrotron-source radiation from two crystal forms of wild-type peroxiredoxin which belonged to the monoclinic space group P2(1) (with unit-cell parameters a = 59.26, b = 68.80, c = 75.71 A, beta = 93.45 degrees) and to the orthorhombic space group P2(1)2(1)2 (with unit-cell parameters a = 64.70, b = 130.73, c = 35.59 A), respectively. Data were also collected to 2.17 A resolution using a home X-ray source from a V152C peroxiredoxin crystal which belongs to the triclinic space group (P1), with unit-cell parameters a = 36.65, b = 41.53, c = 58.06 A, alpha = 70.52, beta = 93.45, gamma = 64.31 degrees. Phases have been obtained using molecular replacement with the structure of human peroxiredoxin V (PDB code 1hd2) as a search model. Refinement of the structures is in progress. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/12198315/Crystallization_and_preliminary_X_ray_data_of_a_bifunctional_peroxiredoxin_from_poplar_ DB - PRIME DP - Unbound Medicine ER -