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Aim. Bacterial expression and isotopic labeling of recombinant EMAP II in preparative scale with the aim to study its spatial structure by NMR spectroscopy. Methods. The recombinant 15N, 13N-labeled EMAP II protein was expressed in Escherichia coli BL21(DE3) pLysE on M9 minimal medium and purified by metal-chelated chromatography on Ni-NTA agarose. Quality of obtained for NMR studies N and 15N/13C-double labeled EMAP II was confirmed by mass spectroscopy and used for preparation of NMR samples. Results. The preparations of 15N and 15N/13C double labelled EMAP II were obtained. The recorded NMR spectra of EMAP II were analyzed. Conclusions. Dispersion of NMR signals in two-dimensional 1H/13C/15N and NHSQC spectra confirm the presence of compact three-dimensional structure of the protein. The NMR samples were stable at least for 5–6 days at chosen conditions. These results will be used as a starting point for determination of high resolution three-dimensional structure of recombinant EMAP II cytokine in solution by NMR spectroscopy

Bacterial expression and 13C/15N isotopic labeling of EMA PII cytokine for structural studies by NMR spectroscopy