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<h3 style="text-align:center"> Dairy</h3>

<h3 style="text-align:center"> Dairy</h3>

                                 <li><a>His-sup</a>: 6.353 mg/ml</li>

                                 <li><a>His-sup</a>: 6.353 mg/ml</li>

                         </ul>

                         </ul>

                             <ul>

                             <ul>

                                 <li>We broke the E.coli with ultrasonication, and extracted 3A-mSA protein using a affinity column. Mixed 3A-mSA and 3B in TBS buffer. Then we did a SDS-PAGE electrophoresis and analysis the results ( Fig.1 ).We could find out that 3A-mSA had the ability to crosslink with 3B.</li>

                                 <li>We broke the E.coli with ultrasonication, and extracted 3A-mSA protein using a affinity column. Mixed 3A-mSA and 3B in TBS buffer. Then we did a SDS-PAGE electrophoresis and analysis the results ( Fig.1 ).We could find out that 3A-mSA had the ability to crosslink with 3B.</li>

                                 <li><a>3A-red</a>: 93.560 mg/ml</li>

                                 <li><a>3A-red</a>: 93.560 mg/ml</li>

                         </ul>

                         </ul>

                             <ul>

                             <ul>

                                 <li>We tried to measure the reaction capacity of the mSA part of the fusion protein with Biotin-Atto 488 which could show autofluorescence. But results were not useful, because there might be some noncovalent interactions between 3 kDa cutoff centrifuge filters and the molecular.</li>

                                 <li>We tried to measure the reaction capacity of the mSA part of the fusion protein with Biotin-Atto 488 which could show autofluorescence. But results were not useful, because there might be some noncovalent interactions between 3 kDa cutoff centrifuge filters and the molecular.</li>

                                 <li>The adsorption capacity of 6A-SUP was tested, even though the data were not parallel, we confirmed that 6A-SUP can absorb uranyl. The highest adsorption rate was 81.56%</li>

                                 <li>The adsorption capacity of 6A-SUP was tested, even though the data were not parallel, we confirmed that 6A-SUP can absorb uranyl. The highest adsorption rate was 81.56%</li>

                         </ul>

                         </ul>

                             <ul>

                             <ul>

                                 <li>Last week we got nothing useful. So we changed the protocol about how to use Biotin-Atto 488. We prepared several little affinity columns, immobilized 3A-mSA containing 6x His-Tag, and perfused the columns with solution of Biotin-Atto 488. After measuring the fluorescence intensity, we got a qualitative result that 3A-mSA can react with biotin.</li>

                                 <li>Last week we got nothing useful. So we changed the protocol about how to use Biotin-Atto 488. We prepared several little affinity columns, immobilized 3A-mSA containing 6x His-Tag, and perfused the columns with solution of Biotin-Atto 488. After measuring the fluorescence intensity, we got a qualitative result that 3A-mSA can react with biotin.</li>

                                 <li>The adsorption capacity of 3A-SUP and 3A-SUP+3B was tested. We confirmed that 3A-SUP can absorb uranyl, so can 3A-SUP+3B. In today’s experiments, the data was more parallel. We used solution containing uranyl only as control and its uranyl concentration after filtration as the actual concentration of uranyl.</li>

                                 <li>The adsorption capacity of 3A-SUP and 3A-SUP+3B was tested. We confirmed that 3A-SUP can absorb uranyl, so can 3A-SUP+3B. In today’s experiments, the data was more parallel. We used solution containing uranyl only as control and its uranyl concentration after filtration as the actual concentration of uranyl.</li>

                         </ul>

                         </ul>

                             <ul>

                             <ul>

                                 <li>To absorb the proteins in the environment, we wanted to use biotin-coated beads. So we bought the reagents and magnetic beads with amino group.</li>

                                 <li>To absorb the proteins in the environment, we wanted to use biotin-coated beads. So we bought the reagents and magnetic beads with amino group.</li>

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                                 <li><a>3A-msa in the form of inclusion body</a>: 2.273 mg/ml</li>

                                 <li><a>3A-msa in the form of inclusion body</a>: 2.273 mg/ml</li>

                                 <li><a>3A</a>: 29.768 mg/ml</li>

                                 <li><a>3A</a>: 29.768 mg/ml</li>

                         </ul>

                         </ul>

                         <li><b>Uranyl Absorption:</b></li>

                         <li><b>Uranyl Absorption:</b></li>

                                 <li>We tested the adsorption capacity of 3/4/6A-SUP and 3/4/6A-SUP+3B in one day to exclude unnecessary effects. Then we analyzed the data and found the results were compromising. The capacity were fair and even though the proteins formed colloid, the adsorption capacity barely decreased.</li>

                                 <li>We tested the adsorption capacity of 3/4/6A-SUP and 3/4/6A-SUP+3B in one day to exclude unnecessary effects. Then we analyzed the data and found the results were compromising. The capacity were fair and even though the proteins formed colloid, the adsorption capacity barely decreased.</li>

                         </ul>

                         </ul>

                             <ul>

                             <ul>

                                 <li>Constructed the biotin-coated beads.</li>

                                 <li>Constructed the biotin-coated beads.</li>

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                     <ul>

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                         </ul>

                         </ul>

                         <li><b>Protein Secretion:</b></li>

                         <li><b>Protein Secretion:</b></li>

                             <ul>

                             <ul>

                         </ul>

                         </ul>

                         <li><b>Protein Purification:</b></li>

                         <li><b>Protein Purification:</b></li>

                             <ul>

                             <ul>

                         </ul>

                         </ul>

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                             <ul>

                         </ul>

                         </ul>

                     </ul>

                     </ul>

                 </div>

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<a href="https://2016.igem.org/Team:Peking/Notebook/Protocol:PCR"><img src="https://static.igem.org/mediawiki/2016/0/09/T--Peking--image_protocol_PCR.png"></a>

<a href="https://2016.igem.org/Team:Peking/Notebook/Protocol:PCR"><img src="https://static.igem.org/mediawiki/2016/0/09/T--Peking--image_protocol_PCR.png"></a>

<p style="text-align:center"><b>PCR</b></p>

<p style="text-align:center"><b>PCR</b></p>

</div>

</div>

<a href="https://2016.igem.org/Team:Peking/Notebook/Protocol:AGE"><img src="https://static.igem.org/mediawiki/2016/5/51/T--Peking--image_protocol_AGE.png"></a>

<a href="https://2016.igem.org/Team:Peking/Notebook/Protocol:AGE"><img src="https://static.igem.org/mediawiki/2016/5/51/T--Peking--image_protocol_AGE.png"></a>

<p style="text-align:center"><b>Agarose Gel Electrophoresis</b></p>

<p style="text-align:center"><b>Agarose Gel Electrophoresis</b></p>

</div>

</div>

<a href="https://2016.igem.org/Team:Peking/Notebook/Protocol:pH_Gradient_Experiment"><img src="https://static.igem.org/mediawiki/2016/9/97/T--Peking--image_protocol_pH_Gradient_Experiment.png"></a>

<a href="https://2016.igem.org/Team:Peking/Notebook/Protocol:pH_Gradient_Experiment"><img src="https://static.igem.org/mediawiki/2016/9/97/T--Peking--image_protocol_pH_Gradient_Experiment.png"></a>

<p style="text-align:center"><b>pH Gradient Experiment</b></p>

<p style="text-align:center"><b>pH Gradient Experiment</b></p>

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