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Comparative Study
. 2009 Feb 1;65(Pt 2):169-72.
doi: 10.1107/S1744309109000153. Epub 2009 Jan 31.

Crystallization and preliminary crystallographic analysis of N-acetyltransferase Mpr1 from Saccharomyces cerevisiae

Affiliations
Comparative Study

Crystallization and preliminary crystallographic analysis of N-acetyltransferase Mpr1 from Saccharomyces cerevisiae

Takao Hibi et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

Mpr1 is an enzyme that catalyzes the N-acetylation of the toxic L-azetidine-2-carboxylic acid (AZC). Recently, Mpr1 has been shown to reduce levels of intracellular reactive oxygen species (ROS) under oxidative stress. The natural substrate involved in the ROS elimination in vivo is still unknown. Mpr1 has been purified and crystallized in space groups P1 and P3(1)12. X-ray data were collected to 1.9 A resolution from a trigonal crystal soaked with AZC.

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Figures

Figure 1
Figure 1
Crystals of Mpr1 from yeast. (a) A single triclinic crystal (form I) obtained by the sitting-drop method. (b) A prism-shaped trigonal crystal (form II) obtained in the presence of MgCl2.
Figure 2
Figure 2
Diffraction image obtained on Photon Factory beamline BL-5A. Diffraction data were collected at a wavelength of 0.9793 Å with a crystal-to-detector distance of 237.8 mm. The resolution at the edges of the image is 1.9 Å.

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