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. 2008 Aug 20;36(17):5441–5450. doi: 10.1093/nar/gkn516

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© 2008 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — (A) Sequence comparison of RAD54 and RAD54B. These proteins are separated into three regions (N-terminal domain, SWI2/SNF2 domain and C-terminal domain), and the amino acid sequence identities and similarities between these proteins were calculated for each region. The amino acid number at the boundary of each domain is denoted. The gray lines indicate the seven helicase motifs (I, Ia, II, III, IV, V and VI, respectively). (B) Purification of the RAD54B_26–225 protein. The peak fractions from the Ni-NTA agarose column (lane 2), the fraction after the removal of the His₆ tag (lane 3), the Benzamidine Sepharose flow-through (lane 4), the Q-Sepharose flow-through (lane 5) and the peak fractions from the SP-Sepharose column (lane 6) were analyzed on a 12% SDS–PAGE gel, which was stained with Coomassie Brilliant Blue. Lane 1 indicates the molecular mass markers. (C) Gel filtration analysis of RAD54B_26–225. The arrow indicates the peak location of a molecular weight marker, ovalbumin (43 kDa), which nearly corresponds to that of RAD54B_26–225.