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![[Figure 2]](jc5035fig2mag.jpg)
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Figure 2
Purification of Sc-Rsm22. (a) Typical SEC elution profile of Sc-Rsm22 showing the presence of two oligomeric forms in the sample. The first peak (minor) and the second peak (major) correspond to higher (dimeric) and lower (monomeric) oligomeric forms of Sc-Rsm22, respectively. SDS–PAGE analysis of Sc-Rsm22 SEC elution fractions is shown at the top. (b) SDS–PAGE analysis of the SEC elution fractions of monomeric Sc-Rsm22. The samples in the SDS–PAGE were the following: molecular-mass standard marker, IMAC elution fraction (IMAC-E) and the SEC elution fractions of monomeric Sc-Rsm22 (peak 2). The bands of purified protein run just below the 75 kDa marker band, which corresponds to a calculated mass of 71.2 kDa for the histidine-tagged Sc-Rsm22 construct used in this study. |
![[Figure 2]](jc5035fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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