POLYMORPHOUS CRYSTALLIZATION AND DIFFRACTION OF THREONINE DEAMINASE FROM ESCHERICHIA-COLI

Authors
GALLAGHER DT EISENSTEIN E FISHER KE ZONDLO J CHINCHILLA D YU HD DILL J WINBORNE E DUCOTE K XIAO GY GILLILAND GL
Citation
Dt. Gallagher et al., POLYMORPHOUS CRYSTALLIZATION AND DIFFRACTION OF THREONINE DEAMINASE FROM ESCHERICHIA-COLI, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 467-469
Citations number
18
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
3
Pages
467 - 469
Database
ISI
SICI code
0907-4449(1998)54:<467:PCADOT>2.0.ZU;2-L
Abstract
The biosynthetic threonine deaminase from Escherichia coli, an alloste ric tetramer with key regulatory functions, has been crystallized in s everal crystal forms. Two distinct forms, both belonging to either spa ce group P3(1)21 or P3(2)21, with different sized asymmetric units tha t both contain a tetramer, grow under identical conditions. Diffractio n data sets to 2.8 Angstrom resolution (native) and 2.9 Angstrom resol ution (isomorphous uranyl derivative) have been collected from a third crystal form in space group I222.