This paper describes the NMR screening of 141 small (<15 kda) recombinant="" thermotoga="" maritima="" proteins="" for="" globular="" folding.="" the="" experimental="" data="" shows="" that="">25% of the screened proteins are folded under our screening conditions, which makes this procedure an important step for selecting those proteins that are suitable for structure determination. A comparison of screening based either on 1D ¹H NMR with unlabeled proteins or on 2D [¹H,¹⁵N]-COSY with uniformly ¹⁵N-labeled proteins is presented, and a comprehensive analysis of the 1D ¹H NMR screening data is described. As an illustration of the utility of these methods to structural proteomics, the NMR structure determination of TM1492 (ribosomal protein L29) is presented. This 66-residue protein consists of a N-terminal 3₁₀-helix and two long -helices connected by a tight turn centered about glycine 35, where conserved leucine and isoleucine residues in the two -helices form a small hydrophobic core.