Crystallization and preliminary X-ray analysis of human MTH1 with a homogeneous N-terminus

Yukari Koga, Miyuki Inazato, Teruya Nakamura, Chie Hashikawa, Mami Chirifu, Asuka Michi, Taku Yamashita, Sachiko Toma, Akihiko Kuniyasu, Shinji Ikemizu, Yusaku Nakabeppu, Yuriko Yamagata

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5 Citations (Scopus)


Human MTH1 (hMTH1) is an enzyme that hydrolyses several oxidized purine nucleoside triphosphates to their corresponding nucleoside monophosphates. Crystallographic studies have shown that the accurate mode of interaction between 8-oxoguanine and hMTH1 cannot be understood without determining the positions of the H atoms, as can be observed in neutron and/or ultrahigh-resolution X-ray diffraction studies. The hMTH1 protein prepared in the original expression system from Escherichia coli did not appear to be suitable for obtaining high-quality crystals because the hMTH1 protein had heterogeneous N-termini of Met1 and Gly2 that resulted from N-terminal Met excision by methionine aminopeptidase from the E. coli host. To obtain homogeneous hMTH1, the Gly at the second position was replaced by Lys. As a result, mutant hMTH1 protein [hMTH1(G2K)] with a homogeneous N-terminus could be prepared and high-quality crystals which diffracted to near 1.1 Å resolution using synchrotron radiation were produced. The new crystals belonged to space group P212121, with unit-cell parameters a = 46.36, b = 47.58, c = 123.89 Å.

Original languageEnglish
Pages (from-to)45-48
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number1
Publication statusPublished - Jan 2013

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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