Tables

Style Use with This Tag Notes
pd_table <table class=”pd_table”> This style is required for all data tables.
pd_gridlines <table class=”pd_table pd_gridlines”> This style is optional, but works in conjunction with the ‘pd_table” class. All specification tables should use both classes.
pd_colorbackground <tr class=”pd_colorbackground”> This class should only be used on every other row in the table. It is the alternate row color.
pd_centeredcell <td class=”pd_centeredcell”> For centered content within a cell.
pd_dividercell <td class=”pd_dividercell”> This class is used when you want an open horizontal space to divide the table.
pd_divider <div class=”pd_divider”> This class is used to create a horizontal rule. It works in conjuction with the “pd_dividercell” class like this:

<td class=”pd_dividercell”>
<div class=”pd_divider”></div>
</td>

Example:

Table 1. Improved processivity, catalytic activity, and thermal stability shown by Taq polymerase and Taq(Δ289), the mutant form of Taq, and a commercially available wild-type Pfu polymerase (adapted from Wang et al. 2004).

Enzyme Processivity (median number of nucleotides incorporated per binding event) Turnover Rate (kcats-1) t1/2 (min) at 97.5°C
Taq (Δ289) 2.9 ± 0.7 18 ± 2 39
Sso7d fusion to Taq (Δ289) 51.0 ± 6 20 ± 1 35
Taq 22 ± 3 21 ± 1 nd
Sso7d fusion to Taq 104 ± 17 20 ± 1 nd
Pfu 6 ± 0.5 3.2 ± 0.1 730
Sso7d fusion to Pfu 55 ± 3 5.7 ± 0.2 789

Performance was measured in the full length Taq (which possesses an 5′-3′ exonuclease domain and a polymerase domain), Taq(Δ289) (which lacks the exonuclease domain and is considered to have less processivity than full length Taq), and Pfu ( a commercially available high-fidelity thermostable polymerase) with and without fusion with Sso7d protein. Processivity (assessed by median number of nucleotides incorporated in a binding event), catalytic activity (as determined by the turnover rate (kcat) of nucleotide incorporation at a saturating amount of dNTPs), and thermal stability (evaluated as half-life (t1/2) of the remaining activity of the enzyme after incubation at 97.5°C) were determined (see Wang et al. 2004 for further details). nd, not determined.

Code
<p><strong>Table 1. Improved processivity, catalytic activity, and thermal stability shown by Taq polymerase and Taq(Δ289), the mutant form of Taq, and a commercially available wild-type Pfu polymerase (adapted from Wang et al. 2004).<br />
</strong></p>
<table class=”pd_table pd_gridlines” width=”100%”>
<tbody>
<tr class=”pd_tableheader”>
<td width=”25%”><strong>Enzyme</strong></td>
<td width=”25%”><strong>Processivity (median number of nucleotides incorporated per binding event)</strong></td>
<td width=”25%”><strong>Turnover Rate (k<sub>cat</sub>s<sup>-1</sup>)</strong></td>
<td width=”25%”><strong>t<sub>1/2</sub> (min) at 97.5°C</strong></td>
</tr>
<tr class=”pd_colorbackground”>
<td>Taq (Δ289)</td>
<td>2.9 ± 0.7</td>
<td>18 ± 2</td>
<td>39</td>
</tr>
<tr>
<td>Sso7d fusion to Taq (Δ289)</td>
<td>51.0 ± 6</td>
<td>20 ± 1</td>
<td>35</td>
</tr>
<tr class=”pd_colorbackground”>
<td>Taq</td>
<td>22 ± 3</td>
<td>21 ± 1</td>
<td>nd</td>
</tr>
<tr>
<td>Sso7d fusion to Taq</td>
<td>104 ± 17</td>
<td>20 ± 1</td>
<td>nd</td>
</tr>
<tr class=”pd_colorbackground”>
<td>Pfu</td>
<td>6 ± 0.5</td>
<td>3.2 ± 0.1</td>
<td>730</td>
</tr>
<tr>
<td>Sso7d fusion to Pfu</td>
<td>55 ± 3</td>
<td>5.7 ± 0.2</td>
<td>789</td>
</tr>
</tbody>
</table>
<p class=”wp-caption”>Performance was measured in the full length Taq (which possesses an 5′-3′ exonuclease domain and a polymerase domain), Taq(Δ289) (which lacks the exonuclease domain and is considered to have less processivity than full length Taq), and Pfu ( a commercially available high-fidelity thermostable polymerase) with and without fusion with Sso7d protein. Processivity (assessed by median number of nucleotides incorporated in a binding event), catalytic activity (as determined by the turnover rate (k<sub>cat</sub>) of nucleotide incorporation at a saturating amount of dNTPs), and thermal stability (evaluated as half-life (t<sub>1/2</sub>) of the remaining activity of the enzyme after incubation at 97.5°C) were determined (<a href=”#references”>see Wang et al. 2004 for further details</a>). nd, not determined.</p>