title: Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-ray analysis.
abstract: 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.
authors.affiliation: Max-Planck-Institut für Biochemie, Abt. Strukturforschung, Am Klopferspitz 18-a, D-82152 Martinsried bei München, Germany. martins@biochem.mpg.de
authors.forename: B M
authors.initials: BM
authors.lastname: Martins
authors.forename: B
authors.initials: B
authors.lastname: Grimm
authors.forename: H P
authors.initials: HP
authors.lastname: Mock
authors.forename: G
authors.initials: G
authors.lastname: Richter
authors.forename: R
authors.initials: R
authors.lastname: Huber
authors.forename: A
authors.initials: A
authors.lastname: Messerschmidt
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D014026:Nicotiana / Q000201:enzymology*; D014575:Uroporphyrinogen Decarboxylase / Q000737:chemistry*
chemical_list: D014575:Uroporphyrinogen Decarboxylase