Open AccessCrystallization and preliminary crystallographic analysis of two eukaryotic fructosyl peptide oxidases
Author(s) -
Ichiyanagi Atsushi,
Hirokawa Kozo,
Gomi Keiko,
Nakatsu Toru,
Kato Hiroaki,
Kajiyama Naoki
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112051445
Subject(s) - monoclinic crystal system , crystallography , tetragonal crystal system , crystallization , chemistry , histidine , peptide , crystal structure , materials science , biochemistry , enzyme , organic chemistry
Fructosyl peptide oxidase (FPOX) catalyses the oxidation of α‐glycated dipeptides such as N α ‐(1‐deoxy‐D‐fructos‐1‐yl)‐L‐valyl‐L‐histidine (Fru‐ValHis) and is used in the diagnosis of diabetes mellitus. Here, two thermostable mutants of FPOX, CFP‐T7 and EFP‐T5M, were crystallized by the sitting‐drop vapour‐diffusion method. The crystal of CFP‐T7 belonged to the tetragonal space group P 4 1 2 1 2, with unit‐cell parameters a = b = 110.09, c = 220.48 Å, and that of EFP‐T5M belonged to the monoclinic space group P 2 1 , with unit‐cell parameters a = 43.00, b = 230.05, c = 47.27 Å, β = 116.99°. The crystals of CFP‐T7 and EFP‐T5M diffracted to 1.8 and 1.6 Å resolution, respectively.