A protein corresponding to the extracellular 1-209 domain of the α-subunit of the nicotine acetylcholine receptor from the electric organ of Torpedo californica was prepared using the corresponding cDNA domain by culturing Escherichia coli cells on a synthetic medium supplemented with 5-fluoro-L-tryptophan. The presence of a (His)6fragment preceding the 1-209 sequence allowed purification of the protein isolated from inclusion bodies by affinity chromatography on Ni-NTA Agarose. The incorporation of 5-fluorotryptophan residues was found by19F NMR to be ∼50%. The spectrum of the protein reduced in the denaturing conditions and subsequently reoxidized in a dilute solution under denaturing conditions in the presence of 0.05% SDS was sufficiently resolved, which allowed partial assignment of19F resonances using the Trp60Phe mutant protein. The ability of the prepared domains to specifically bind snake α-neurotoxins was demonstrated with the use of radioiodinated α-bungarotoxin and trifluoroacetylated α-cobratoxin.