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Humboldt-Universitaet zu Berlin - Structural Biology / Biochemistry

Humboldt-Universitaet zu Berlin | Department of Biology | Structural Biology / Biochemistry | Publications | Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-ray analysis.

Berta M Martins, Bernhard Grimm, Hans-Peter Mock, Robert Huber, and Albrecht Messerschmidt (2001)

Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-ray analysis.

Acta Crystallographica Section D Biological Crystallography, 57(11):1709-11.

Uroporphyrinogen-III decarboxylase from Nicotiana tabacum is a plastidial enzyme involved in the biosynthesis of chlorophyll and haem. Sedimentation equilibrium with protein producing diffracting crystals clearly indicates that the enzyme is a homodimer under similar ionic strength conditions to those found in the chloroplast stroma. Additionally, dynamic light scattering reveals an ionic strength dependence for this oligomerization state. Crystals were obtained in the hexagonal space group P622 with one molecule per asymmetric unit and diffracted to 2.3 A resolution using synchrotron radiation.