Polymorphous crystallization and diffraction of threonine deaminase from Escherichia coli

Journal Article

The biosynthetic threonine deaminase from Escherichia coli, an allosteric tetramer with key regulatory functions, has been crystallized in several crystal forms. Two distinct forms, both belonging to either space group P3121 or P3221, with different sized asymmetric units that both contain a tetramer, grow under identical conditions. Diffraction data sets to 2.8 Å resolution (native) and 2.9 Å resolution (isomorphous uranyl derivative) have been collected from a third crystal form in space group I222.

Full Text

Duke Authors

Cited Authors

  • Gallagher, DT; Eisenstein, E; Fisher, KE; Zondlo, J; Chinchilla, D; Yu, HD; Dill, J; Winborne, E; Ducote, K; Xiao, G; Gilliland, GL

Published Date

  • May 1, 1998

Published In

Volume / Issue

  • 54 / 3

Start / End Page

  • 467 - 469

Published By

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444997011360