Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-l-methionine transferase protein TehB from Escherichia coli

The E. coli TehB methyltransferase has been purified and crystallized in the presence of SAM and sinefungin. Diffraction data have been collected to 1.9 Å resolution for both complexes. TehB is an S-adenosyl-l-methionine (SAM) dependent methyltransferase that detoxifies tellurite in bacteria. The Escherichia coli TehB protein was purified and crystallized in the presence of both SAM and sinefungin. The TehB–SAM and TehB–sinefungin crystals both diffracted X-rays to 1.9 Å resolution. The TehB–SAM crystals belonged to space group C2, with unit-cell parameters a = 60.0, b = 56.1, c = 130.6 Å, β = 97.9°. The TehB–sinefungin crystals belonged to space group P2₁, with unit-cell parameters a = 59.1, b = 55.5, c = 129.7 Å, β = 95.9°