2.1.1.200	crystal structure of the catalytic domain	
2.1.1.200	purified recombinant C-terminally His6-tagged wild-type enzyme, hanging drop vapour diffusion method, mixing of 10 mg/ml of protein 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM MgCl2, and 2 mM S-adenosyl-L-homocysteine, with 3.6 M NaCl and 0.1 M HEPES, pH 8.2, 20°C, 2 months, X-ray diffraction structure determination and analysis, full-length EcTrmJ forms an unusual dimer in the asymmetric unit, with both the catalytic SPOUT domain and C-terminal extension forming separate dimeric associations in the crystal structure, molecular replacement	
2.1.1.200	recombinant TrmJ-NTD protein, hanging drop vapour diffusion method, mixing of 0.001 ml of 20 mg/ml protein solution with 0.002 ml of reservoir solution containing Bis-Tris propane, pH 6.5, 0.2 M ammonium chloride, 25% w/v PEG 3350, 20°C, or with 0.03 M MgCl2, 0.03 M CaCl2, 20% w/v PEG MME550, 10% w/v PEG 20000, and 0.1 M MOPS/Na-HEPES, pH 7.5, and soaking with 1 mM sinefungin, 20°C, resulting in two different crystal forms, method optimization, X-ray diffraction structure determination and analysis at 1.7 A and 1.8-2.2 A resolution, respectively