@article{oai:repo.qst.go.jp:00049515,
 author = {中村, 照也 and 平田, 啓介 and 藤宮, 佳奈 and 池鯉鮒, 麻美 and 有森, 貴夫 and 玉田, 太郎 and 池水, 信二 and 山縣, ゆり子 and 玉田 太郎},
 issue = {1},
 journal = {Int. J. Microgravity Sci. Appl.},
 month = {Jan},
 note = {Human MTH1 hydrolyzes oxidized nucleoside triphosphates with broad substrate specificity and draws attention as a potential anticancer
target. Recently, we determined the high resolution crystal structures of MTH1 and suggested that MTH1 recognizes different substrates via an
exchange of the protonation state at Asp119 and Asp120. In order to validate this mechanism, it is essential to observe hydrogen atoms by
ultra-high resolution X-ray crystallography and/or neutron crystallography using large high quality crystals. Here we carried out the
crystallization of MTH1 in complex with a substrate, 8-oxo-dGTP, under microgravity in the Japanese Experiment Module ‘Kibo’. One of the
crystals diffracted to 1.04-Å resolution, which is better than that we reported previously. We carried out bond length analysis of Asp119 and
Asp120 using this updated data, which revealed the protonation state based on the bond lengths with higher accuracy and precision.},
 title = {X-ray Structure Analysis of Human Oxidized Nucleotide Hydrolase MTH1 using Crystals Obtained under Microgravity},
 volume = {36},
 year = {2019}
}