update dcddh

wiki/pages/dcddh.html

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                         Protein overexpression was induced according to the following conditions (see Table 1). 
                         The best overexpression conditions were those of row two in Table 1 (see below). 
                         We used a plasmid containing the gene for IF3 as a control in the case of overexpression with the pET24a vector a positive control. 
-                        We chose IF3 as a control because of confirmed clear overexpression bands at 24 kDa (Forster <em>et al</em>. 1977) (see Figure 5). 
+                        We chose IF3 as a control because of confirmed clear overexpression bands at 24 kDa (Forster <em>et al</em>. 2001) (see Figure 5). 
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                       <p>The construct contained a tag for a polyhistidine tag for purification via an imidazole elution gradient at Testa Center after induction of overexpression. 
-                        The aim of working at Testa Center was to obtain a higher yield of purified DCDDH enzyme than that obtained in the lab (a shift from µg amount to mg amounts). 
+                        he aim of working at Testa Center was to obtain a higher yield of purified TphB enzyme than that obtained in the lab (a shift to mg amount versus µg amount). 
                         Overexpression clones were grown after inoculation of SOB in bioreactors generously provided by Testa Center. 
-                        After an overnight culture was grown, cells were harvested, lysed, and the supernatant collected. 
-                        This was then submitted to a nickel affinity column for elution of protein via an imidazole gradient from 25mM to 500mM. 
-                        No purified product was obtained, most likely due to a sharp drop in cell growth after 5 minutes within the bioreactor (see Figure 6).
-                        <br><br>
+                        <br><br>After an overnight culture was grown, cells were harvested, lysed, and the supernatant collected. This was then submitted to a nickel affinity column for elution of protein via an imidazole gradient from 25mM to 500mM. 
+                        No purified product was obtained due to a sharp drop in cell growth after 5 minutes within the bioreactor (see Figure 6). 
                         The scale up likely failed due to a lack of established information about optimal growth conditions for DCDDH. 
-                        There is no documented toxicity of the enzyme but the cells may have stopped growing due to internal pressures exerted on other cellular metabolic pathways by DCDDH. 
-                        It may be that the enzyme began to inhibit normal processes of cellular respiration or perhaps interfered with functions of other proteins.  
-                        </p>    
+                        There is no documented toxicity of the enzyme but the cells may have stopped growing due to internal pressures exerted on other cellular metabolic pathways by DCDDH. It may be that the enzyme began to inhibit normal processes of cellular respiration or perhaps interfered with functions of other proteins.  
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                             <img style="width: 40%;" src='https://static.igem.wiki/teams/4378/wiki/img/lab-enzymes/dcddh/dcddh-bioreactor.png' alt="Growing status and conditions in bioreactor for DCDDH transformed BL21">