Nature research paper: Structural basis for directional chitin biosynthesis
. The microtitre plates were coated with wheat germ agglutinin and blocked with bovine serum albumin blocking buffer. The plates were stored at −20 °C for further assays. The plates were emptied by centrifugation before usage. Next, 50 μl of the reaction mixture was added to each well followed by 50 μl of enzyme suspension to a final volume of 100 μl. After incubation at 30 °C for 1 h, the plates were emptied and washed three times.
. The specific enzyme activity was expressed as nmol GlcNAc per µg protein per hour. Each test was repeated three times.Chs1, 4.5 µM to 10 mM UDP-GlcNAc, 50 mM Tris-HCl buffer and 150 mM NaCl were incubated in a final volume of 100 µl in the absence or presence of 1 mM GlcNAc. The data were analysed by GraphPad Prism software.
For confocal laser scanning microscopy, reaction samples were incubated with wheat germ agglutinin coupled to fluorescein isothiocyanate for 15 min. After washing five times with distilled water, the samples were imaged for fluorescein isothiocyanate fluorescence using an LSM 880 laser scanning confocal microscope and appropriate filter sets .
ATR-FTIR spectra and X-ray diffraction were used to determine the crystal isomorph of synthesized chitin. Chitin derived from shrimp and chitin derived fromwere used as reference samples for α-chitin and β-chitin, respectively. FTIR spectra were obtained using a Nicolet iS5 FTIR Spectrometer with a diamond ATR unit over the frequency range of 4,000 to 600 cmand 128 scans. The data were analysed with Omnic software.
at a magnification of ×22,500, resulting in a physical pixel size of 1.07 Å. The exposure time for each stack of 32 frames was 3.43 s, corresponding to a total dose of approximately 60 e
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