Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola.
New method of purification of tyrosine phenol-lyase from Erwinia herbicola has been developed. The enzyme obtained is homogeneous and characterised by a specific activity which is three times higher then that described earlier. Crystals of holoenzyme complexed with monovalent cations have been grown from NaCl, KCl and (NH4)2SO4 containing solutions. The crystals belong to P6(2)22 space group. They are stable to the X-ray radiation and diffract up to 2.6-3.1 A. Asymmetric unit contains one subunit of tetrameric molecule.
Pletnev
S V
SV
Shubnikov Institute of Crystallography, Russian Academy of Sciences, Moscow, Russia.
Isupov
M N
MN
Dauter
Z
Z
Wilson
K S
KS
Faleev
N G
NG
Harutyunyan
E G
EG
Demidkina
T V
TV
D003460:Crystallization; D018360:Crystallography, X-Ray; D004885:Erwinia / Q000201:enzymology*; D011487:Protein Conformation; D014447:Tyrosine Phenol-Lyase / Q000737:chemistry* / Q000302:isolation & purification*
D014447:Tyrosine Phenol-Lyase