2.1.1.179	in complex with S-adenosylhomocysteine. An N-terminal domain surface within RmtC, comprising basic residues from both the N1 and N2 subdomains, directly contributes to 30S-binding affinity. Additional residues lining a contiguous adjacent surface on the C-terminal domain are critical for 16S rRNA modification but do not directly contribute to the binding affinity	
2.1.1.179	purified Sgm is complexed with 5 mM of the cofactors S-adenosylmethionine/S-adenosylhomocysteine. Crystallization trials are carried out at room temperature by hanging-drop vapor-diffusion method, structure of Sgm in complex with cofactors S-adenosylmethionine and S-adenosylhomocysteine is determined at 2.0 A and 2.1 A resolution, respectively	
2.1.1.179	RmtB containing S-adenosyl-L-homocysteine in the active site