Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin
Han, Huijong; Kursula, Petri (2017-03-06)
Huijong Han, Petri Kursula, Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin, In Data in Brief, Volume 11, 2017, Pages 552-556, ISSN 2352-3409, https://doi.org/10.1016/j.dib.2017.02.049.
© 2017 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
We present datasets that can be used for the experimental phasing of crystal structures of two myelin proteins. The structures were recently described in the articles “Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping” (H. Han, P. Kursula, 2014)  and “The olfactomedin domain from gliomedin is a β-propeller with unique structural properties” (H. Han, P. Kursula, 2015) . Crystals of periaxin were derivatized with tungsten and xenon prior to data collection, and diffraction data for these crystals are reported at 3 and 1 wavelengths, respectively. Crystallographic data for two different pressurizing times for xenon are provided. Gliomedin was derivatized with platinum, and data for single-wavelength anomalous dispersion are included. The data can be used to repeat the phasing experiments, to analyze heavy atom binding sites in proteins, as well as to optimize future derivatization experiments of protein crystals with these and other heavy-atom compounds.
- Avoin saatavuus