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Crystallization (Commentary)
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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
757224
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
705988
2.1.1.179
RmtB containing S-adenosyl-L-homocysteine in the active site
712741
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