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View full-text article in PMC

. 2013 Nov 6;8(11):e78216. doi: 10.1371/journal.pone.0078216

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© 2013 Yonekura et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) An SDS-PAGE pattern of isolated protein solution and crystals of the Hfq and catalase HPII complex dissolved in SDS buffer solution. Lanes are: 1, markers; 2, protein solution after nickel-affinity chromatography; and 3, crystals of Hfq and HPII complex. Arrows and numbers in lane 3 indicate samples for PMF MALDI-TOF analysis. Asterisk in lane 2 indicates an overproduced PomA protein with a histidine tag. Bands 1 and 2 were identified as dimer and monomer of HPII and bands 3 and 4 as hexamer and monomer of Hfq by the PMF analysis, respectively. Note that the fraction eluting from the nickel-affinity column contained significant amounts of both Hfq and HPII. (B) Typical electron micrographs of complexes of endogenous Hfq and HPII prepared with negative staining. Some ring-like structures with dimensions of 70 – 80 Å are indicated with arrows. Bar indicates 100 Å.