Purification, crystallization and preliminary X-ray analysis of human histidine decarboxylase.
The core domain of a human histidine decarboxylase mutant was purified and cocrystallized with the inhibitor L-histidine methyl ester. Using synchrotron radiation, a data set was collected from a single crystal at 100 K to 1.8 Å resolution. The crystal belonged to space group C2, with unit-cell parameters a = 215.16, b = 112.72, c = 171.39 Å, β = 110.3°. Molecular replacement was carried out using the structure of aromatic L-amino-acid decarboxylase as a search model. The crystal contained three dimers per asymmetric unit, with a Matthews coefficient (V(M)) of 3.01 Å(3) Da(-1) and an estimated solvent content of 59.1%.
Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan. komori@sci.u-hyogo.ac.jp
Hirofumi
H
Komori
Yoko
Y
Nitta
Hiroshi
H
Ueno
Yoshiki
Y
Higuchi
D003460:Crystallization; D018360:Crystallography, X-Ray; D006640:Histidine Decarboxylase / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D055503:Protein Multimerization
D006640:Histidine Decarboxylase