Polymorphous crystallization and diffraction of threonine deaminase from Escherichia coli.
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 A resolution (native) and 2. 9 A resolution (isomorphous uranyl derivative) have been collected from a third crystal form in space group I222.
Center for Advanced Research in Biotechnology of the University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, USA. travis@dtg.nist.gov
D T
DT
Gallagher
E
E
Eisenstein
K E
KE
Fisher
J
J
Zondlo
D
D
Chinchilla
H D
HD
Yu
J
J
Dill
E
E
Winborne
K
K
Ducote
G
G
Xiao
G L
GL
Gilliland
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D013913:Threonine Dehydratase / Q000737:chemistry*; D014961:X-Ray Diffraction
D013913:Threonine Dehydratase