Journal:

Article Title: Dynamics of Bacterial Community Composition and Activity during a Mesocosm Diatom Bloom

doi:

Figure Lengend Snippet: DGGE profiles of the bacterial community composition over time in tanks 1 and 3. Separate gels (each with 30 to 46% denaturant gradients) were used for the two tanks. Each excised, cloned, and sequenced band is numbered on the left. The relationships of excised band sequences to other sequences in the GenBank database are indicated in the table under the gels.

Article Snippet: Electrophoresis was performed with a hot-bath denaturing gradient gel electrophoresis (DGGE) unit (CBS Scientific, Del Mar, Calif.) using 0.5× TAE running buffer (20 mM Tris, 10 mM acetate, 0.5 mM Na 2 -EDTA, pH 8.2) at 60°C for 5.5 h at 200 V. Gels were stained for 30 min in SYBR Green I nucleic acid stain (Molecular Probes), destained for 10 min in 0.5× TAE, and photographed with UV transillumination.

Techniques: Clone Assay

Journal: Nature Communications

Article Title: The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate

doi: 10.1038/ncomms1797

Figure Lengend Snippet: ( a ) Intersubunit interaction around Arg243. Hydrogen bond and CH/ π stacking are indicated by dashed magenta and orange lines, respectively. ( b ) The ion bridge interaction of Lys249. Dashed cyan line represents ion bridges. ( c , d ) Mutational effect of the residues that participated in the interaction of Arg243 ( c ) and Lys249 ( d ) for the inactivation time constants. The inactivation time constants were measured from the current traces elicited by step pulses from holding potential at −140 mV. The time constant of NavSulP wild type (closed circle, n =8), R243E (open circle, n =4), Y242A (closed triangle, n =6), Y242F (open triangle, n =5), T239V (closed square, n =5) and R243A (open square, n =4) are represented in ( c ). The time constant of NavSulP wild type (closed circle, n =8), K249E (open circle, n =5), E251K (closed triangle, n =4), E254K (open triangle, n =4) and E251K/E254K (open square, n =4), are represented in ( d ). All values are presented as mean±standard error. ( e ) Sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis of tetramer and monomer fractions of NavSulP wild-type (WT) and mutants in size-exclusion chromatography. T and M indicate the tetramer and monomer fractions of NavSulP proteins in size-exclusion chromatography, respectively. To evaluate the amount of protein, proteins were denatured to monomers by sodium dodecyl sulphate treatment. The band intensities of the T and M lanes represent the amount of tetrameric channels and dissociated monomers, respectively. Most NavSulPΔC239 were dissociated to monomers and unable to form channel tetramers.

Article Snippet: Purified proteins were resolved on 7.5–20% sodium dodecyl sulphate-polyacrylamide gel electrophoresis gradient gels (Wako) and stained with silver staining.

Techniques: Polyacrylamide Gel Electrophoresis, Size-exclusion Chromatography