| Autor: |
Sevilla, Francisca, Barranco-Medina, Sergio, Bernier-Villamor, Laura, López-Jaramillo, Francisco Javier, Lázaro, Juan-Jos |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section F (Wiley-Blackwell); Jul2006, Vol. 62 Issue 7, p695-698, 4p, 2 Color Photographs, 1 Diagram, 1 Chart, 1 Graph |
| Abstrakt: |
A cDNA encoding an open reading frame of 199 amino acids corresponding to a type II peroxiredoxin from Pisum sativum with its transit peptide was isolated by RT-PCR. The 171-amino-acid mature protein (estimated molecular weight 18.6 kDa) was cloned into the pET3d vector and overexpressed in Escherichia coli. The recombinant protein was purified and crystallized by the hanging-drop vapour-diffusion technique. A full data set (98.2% completeness) was collected using a rotating-anode generator to a resolution of 2.8 Å from a single crystal flash-cooled at 100 K. X-ray data revealed that the protein crystallizes in space group P1, with unit-cell parameters a = 61.88, b = 66.40, c = 77.23 Å, α = 102.90, β = 104.40, γ = 99.07°, and molecular replacement using a theoretical model predicted from the primary structure as a search model confirmed the presence of six molecules in the unit cell as expected from the Matthews coefficient. Refinement of the structure is in progress. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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