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Crystallization and crystal data on tyrosine phenol‐lyase
Author(s) -
Demidkina T.Y.,
Myagkikh I.V.,
Antson A.A.,
Harutyunyan E.H.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80774-9
Subject(s) - crystallization , chemistry , ammonium sulfate , crystal (programming language) , lyase , crystallography , enzyme , molecule , tyrosine , phenol , crystal growth , stereochemistry , organic chemistry , biochemistry , computer science , programming language
Crystals of the apoenzyme of tyrosine phenol‐lyase (EC 4.1.99.2), a pyridoxal 5′‐phosphate‐dependent enzyme from Citrobacter intermedius , have been grown by vapor diffusion of an ammonium sulfate solution to a protein solution. The crystals belong to space group P2 1 2 1 2, with dimensions of a = 75.5 Å, b = 138.4 Å and c = 94.1 Å and diffract up to 2.7 Å resolution. The asymmetric unit contains one half of the enzyme tetrameric molecule. Two heavy‐atom derivatives of the crystals have been obtained.