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. Author manuscript; available in PMC: 2011 Aug 16.
Published in final edited form as: Methods Mol Biol. 2009;535:135–163. doi: 10.1007/978-1-59745-557-2_9

Fig. 9.2.

Fig. 9.2

Conversion of the SAM-I riboswitch to a sequence that was successfully crystallized. (A) Raw sequence of the SAM-I riboswitch aptamer domain that controls the metF-H2 operon in T. tencongensis. The box encloses all sequence elements that are >90% conserved across phylogeny and implicated in ligand binding. (B) Sequence of the RNA that was crystallized complexed with S-adenosylmethionine. VR1, VR2, and VR3 denote the three regions of the P1, P3, and P4 helices that contained expansions to create a library of different variants of the SAM-I aptamer domain.