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Crystallization and improvement of crystal quality for X-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues by Masanori Kobayashi; Michio Kubota; Yoshiki Matsuura is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Crystallization and improvement of crystal quality for X-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues about?

Maltooligosyl trehalose synthase, one of the two enzymes in the coupled trehalose biosynthesis system in Sulfolobus acidocaldarius, has been puri®ed and crystallized. The chemical modi®cation of this enzyme by reductive methylation of lysine residues signi®cantly improved the crystal quality for X-ray diffraction experiments. The crystals of the modi®ed enzyme belong to orthorhombic space group P2 1 2 1 2 1 , with unit-cell parameters a = 56.70, b = 140.1, c = 205.2 A Ê measured at cryo-temperature, and are found to contain two enzyme molecules per asymmetric unit.

Who reads Crystallization and improvement of crystal quality for X-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues?

Author

Masanori Kobayashi; Michio Kubota; Yoshiki Matsuura

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)