diff --git a/pages/project/results.html b/pages/project/results.html
index 5a33423..127da9b 100644
--- a/pages/project/results.html
+++ b/pages/project/results.html
@@ -4,7 +4,7 @@
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 	<meta name="viewport" content="width=device-width, initial-scale=1.0">
-	<title>iDEC NEFU_China 2023</title>
+	<title>iDEC NEFU_China 2022</title>
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@@ -53,7 +53,7 @@
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-						<a class="chapter-nav " href="https://idec-teams.github.io/2023_NEFU_China/">
+					<a class="chapter-nav " href="../../static/home.html">
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@@ -73,7 +73,7 @@
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-						<a href="../team/mumbers.html" class="dropdown-page cool-link2">
+						<a href="../team/members.html" class="dropdown-page cool-link2">
 							Members
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@@ -159,38 +159,60 @@ <h1>RESULTS</h1>
 		<aside class="sticky">
 			<div id="sub-nav" class="sub-navigation-content">
 				<div class="sub-navigation-chapter cool-link2">
-					<a class="main-nav-link" linkedidchapter="slide1-chapter1">Objectives</a>
+					<a class="main-nav-link" linkedidchapter="slide1-chapter1">Construction of hmaS mutant library</a>
 					<!------Chapter one -->
 				</div>
 				<div class="sub-navigation-chapter cool-link2">
-					<a class="main-nav-link" linkedidchapter="slide1-chapter2">Results</a>
+					<a class="main-nav-link" linkedidchapter="slide1-chapter2">Construction and Test of a Dual-Module
+						Screening Platform</a>
 					<!------Chapter Two -->
 				</div>
 				<div class="sub-navigation-chapter cool-link2">
-					<a class="main-nav-link" linkedidchapter="slide1-chapter3">
-						<li class="t">Construction of biosensors</li>
+					<a class="main-nav-link" linkedidchapter="slide2-chapter2">
+						<li class="t">Functional testing</li>
 					</a>
 					<!------Chapter Three -->
 				</div>
 				<div class="sub-navigation-chapter cool-link2">
-					<a class="main-nav-link" linkedidchapter="slide1-chapter4">
-						<li class="t">Construction of mutant libraries</li>
+					<a class="main-nav-link" linkedidchapter="slide2-chapter3">
+						<li class="t">Screening to obtain excellent mutants</li>
 					</a>
 					<!------Chapter Three -->
 				</div>
 				<div class="sub-navigation-chapter cool-link2">
-					<a class="main-nav-link" linkedidchapter="slide1-chapter5">
-						<li class="t">Outcomes of the dual selections</li>
+					<a class="main-nav-link" linkedidchapter="slide3-chapter1">Modeling and Molecular Docking</a>
+					<!------Chapter Two -->
+				</div>
+				<div class="sub-navigation-chapter cool-link2">
+					<a class="main-nav-link" linkedidchapter="slide4-chapter1">Engineering an E. coli chassis with
+						High-HPP Production</a>
+					<!------Chapter Two -->
+				</div>
+				<div class="sub-navigation-chapter cool-link2">
+					<a class="main-nav-link" linkedidchapter="slide4-chapter2">
+						<li class="t">Overexpression of Key Genes to Enhance the
+							Precursor
+							Supply</li>
 					</a>
 					<!------Chapter Three -->
 				</div>
 				<div class="sub-navigation-chapter cool-link2">
-					<a class="main-nav-link" linkedidchapter="slide1-chapter6">
-						<li class="t">Structure modeling and ligand
-							docking</li>
+					<a class="main-nav-link" linkedidchapter="slide4-chapter3">
+						<li class="t">Functional testing</li>
+					</a>
+					<!------Chapter Three -->
+				</div>
+				<div class="sub-navigation-chapter cool-link2">
+					<a class="main-nav-link" linkedidchapter="slide4-chapter4">
+						<li class="t">Screening to obtain excellent mutants</li>
 					</a>
 					<!------Chapter Four -->
 				</div>
+				<div class="sub-navigation-chapter cool-link2">
+					<a class="main-nav-link" linkedidchapter="slide5-chapter1">Evaluation of Metabolic Engineering and
+						Directed Evolution</a>
+					<!------Chapter Two -->
+				</div>
 
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 				<div id="to-top-arrow">
@@ -206,58 +228,280 @@ <h1>RESULTS</h1>
 					<div class="main-body">
 						<div class="main-body-content">
 							<div id="slide1-chapter1">
-								
+								<h2>Construction of hmaS mutant library</h2>
+								<p>Based on error-prone PCR, we used a low-fidelity DNA polymerase and adjusted
+									Mn<sup>2+ </sup>and
+									Mg<sup>2+</sup>>concentrations and ratio to
+									manipulate the mutation rate. We determined the final concentrations of 0.02 mM
+									Mn<sup>2+</sup>
+									and 0.5 mM Mg<sup>2+</sup> for mutagenesis and
+									achieved a mutation rate of 2 mutations/kb, producing a high variety of
+									mutations.
+									We optimized the Golden Gate assembly
+									procedure to increase the probability of inserting mutated fragments into
+									the
+									vector. Eventually, we constructed a
+									mutant library containing 1 * 10<sup>5</sup> clones (Fig. 1) and the rate of
+									positive clones
+									was 100%.</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/图片1.png" alt="">
+									<p>gY9s-HmaSmut-Bio177 mutant library plates</p>
+								</div>
+
+								<p><b>Figure 1.</b> A mutant library with 10⁵ clones was constructed by using a
+									low-fidelity DNA polymerase, determining the concentrations
+									of 0.02 mM Mn2+ and 0.5 mM Mg2+and the optimized Golden Gate assembly procedure.</p>
 							</div>
 							<div id="slide1-chapter2">
-								
-								<div class="figure-container" style="width: 60%;margin: 0 auto;"">
-										<img src=" ../../static/result/fig1.jpg" alt="">
+								<h2>Construction and Test of a Dual-Module Screening Platform</h2>
+								<p>
+									<b id="slide2-chapter2">Functional testing</b>
+								</p>
+								<p>We used bacteria harboring the Bio177 plasmid to simulate the scenario of low
+									activity, and bacteria containing the
+									gY9s-HmaS-Bio177 plasmid for high enzyme activity to test the functionality of
+									dual-module screening platform. Both
+									strains were spread on selection plates containing 0.01, 0.05 and 0.1 mg/L 5-FC to
+									simulate the screening process under
+									stress conditions (Fig. 2). We found that, in medium with 0.01 mg/L 5-FC, all 10
+									randomly selected clones were verified
+									as positive by colony PCR, yielding a 100% selection rate to distinguish desirable
+									hmaS-containing clones from others.
+									Under condition of 0.05 mg/L 5-FC, the growth of the wild-type HmaS strain was
+									inhibited, resulting in a reduced colony
+									number on the plate. Ultimately, the WT strain could not grow under 0.1 mg/L 5-FC
+									condition.</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/图片2.png" alt="">
+									<p>0.01 mg/L 5-FC 0.05 mg/L 5-FC 0.1 mg/L 5-FC </p>
+								</div>
+								<p><b>Figure 2.</b> Spread strains on selection plates containing 0.01, 0.05 and 0.1
+									mg/L of 5-FC to simulate the screening process under
+									stress conditions.</p>
+
+								<p>
+									<b id="slide2-chapter3">Screening to obtain excellent mutants</b>
+								</p>
+								<p>We transferred the bacterial cultures into the selection media and cultivated the
+									bacteria at 30°C until the bacteria
+									reached the exponential phase (OD<sub>600</sub> =0.2 or 0.6). With increased 5-FC
+									concentrations, the selection pressure
+									accelerated, which enhanced the performance of viable individuals, improved HMA
+									production, and reduced fluorescence
+									strength. Based on colony fluorescence and HMA production, we screened clones under
+									the conditions of 0.6 g/L HPP and
+									0.3 mg/L 5-FC (Fig. 3). And we found a mutant clone hmaS<sup>V152G</sup> that HMA
+									production of
+									mutant clones could increase up to
+									125% compared to that of WT (Fig. 4).</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/t10.jpg" alt="">
 								</div>
-							
-								<div class="figure-container" style="width: 90%;margin: 0 auto;">
-									<img src=" ../../static/result/fig2.png" alt="">
+								<p><b>Figure 3.</b>Graph of the correlation between 5-FC concentration in the medium and
+									HMA production. The orange bars represent HMA
+									levels and blue line depicts fluorescence intensity.</p>
+
+								<p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/t8.jpg" alt="">
 								</div>
-								
+								<p><b>Figure 4.</b>Graph of HMA production by the bacteria harboring
+									HmaS<sup>WT</sup>and
+									HmaS<sup>V152G</sup>clones. With 9 mM HPP as the substrate for
+									whole-cell catalysis, HMA accumulation by the gY9s-HmaS<sup>V152G</sup>-Bio177 and
+									gY9s-HmaS<sup>WT</sup>-Bio177 strains was monitored for 3
+									h.</p>
+
+								<p>
 							</div>
-							<div id="slide1-chapter4" style="margin-bottom:10%;">
-								
-								<div class="figure-container" style="width: 100%;margin: 0 auto;"">
-										<img src=" ../../static/result/fig3.jpg" alt="">
+							<div id="slide3-chapter1">
+								<h2>Modeling and Molecular Docking</h2>
+								<p>We employed the Alphafold2 for homology modeling of both the HmaS<sup>WT</sup>
+									and mutant
+									HmaS<sup>V152G</sup> (Fig. 5).</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/图片3.jpg" alt="">
 								</div>
-								
-								<div class="figure-container" style="width: 90%;margin: 0 auto;"">
-										<img src=" ../../static/result/fig4.png" alt="">
+								<p><b>Figure 5.</b> The surface models for the spatial structures of the
+									HmaS<sup>WT</sup> and
+									HmaS<sup>V152G</sup> mutants in the binding domain of HmaS. The
+									residue 152 is colored in dark blue. The V152G mutation alters the positions of
+									adjacent residues and subsequently
+									increases the wideness of the pocket to easily accommodate HPP molecules.</p>
+								<p>we used the Autodock Vina to dock the HPP molecule to HmaS proteins. The docking
+									energy of HPP with WT and V152G mutant
+									was determined as -3.8 and -4.7 kcal/mol, respectively, indicating that HPP is
+									likely better oriented towards the HmaS
+									mutant. Following docking analysis, we evaluated the ligand-protein interactions
+									using Pymol and Ligplus. After HPP
+									docking with HmaS<sup>V152G</sup>, HPP forms hydrogen bonds with D154, G199 and
+									A204, and
+									engages in hydrophobic interactions with
+									L153, G203, T206 and R318 (Fig. 6)</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/图片4.jpg" alt="">
 								</div>
-								
-								<div class="figure-container" style="width: 60%;margin: 0 auto;"">
-										<img src=" ../../static/result/fig5.jpg" alt="">
+								<p><b>Figure 6.</b>Simulated structures of HmaS<sup>V152G</sup>-HPP binding analyzed
+									by Pymol
+									and Ligplus. Compared to HmaS<sup>WT</sup>
+									and mutant, HmaS<sup>V152G</sup> uses G152,
+									L154 and E199 to form additional hydrogen bonds with a HPP molecule.</p>
+
+								<p>
+							</div>
+							<div id="slide4-chapter1">
+								<h2>Engineering an E. coli chassis with High-HPP Production</h2>
+								<p>
+									<b id="slide4-chapter2"> Overexpression of Key Genes to Enhance the
+										Precursor
+										Supply</b>
+								</p>
+								<p>we constructed the pSB1c-aroG<sup>fbr</sup>-tktA-ppsA (<i>pATP</i>) plasmid to
+									overexpress the
+									phosphoenol-pyruvate synthase (<i>ppsA</i>) gene,
+									the transketolase (<i>tktA</i>) gene and aro<i>G<sup>fbr</sup></i>gene.
+									Through the modifications of
+									genetic
+									overexpression, we obtained a host
+									strain that could produce up to 0.72 g/L HPP.</p>
+								<p>
+									<b id="slide4-chapter3">Building Multi-level Inhibition Platform Based on
+										CRISPRi</b>
+								</p>
+								<p>
+									<strong id="slide4-chapter4">
+										Functional testing</strong>
+								</p>
+								<p>To test the feasibility of multi-level interference, we co-transformed <i>E.
+										coli</i>
+									BW25113 with R6K-dCas9-eGFP plasmid
+									containing the sgRNA targeting the eGFP coding sequence (+40bp) and
+									pYB1a-eGFP
+									plasmid. We tested the effectiveness of
+									sgRNAs with different mismatches in mediating eGFP suppression. The eGFP
+									repression
+									levels is from 6.2% to 80.3% (Fig.
+									7).</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/图片5.tif" alt="">
+								</div>
+								<p><b>Figure 7.</b>Bar graph of the Inhibitory efficiency by the random
+									double-mismatched eGFP-sgRNAs. Fi means fully interference,
+									transformed into the strain that containing the non-mutated R6K-dCas9-eGFP
+									plasmid, which had CA in the 7-8bp spacer of
+									the sgRNA.</p>
+								<p>
+								<p>
+									<strong id="slide4-chapter5">
+										Screening to obtain excellent mutants</strong>
+								</p>
+								<p>We individually co-transformed the plasmids of these R6K-dCas9-sgRNA single
+									or
+									four mismatch sgRNA libraries and
+									non-mismatch sgRNA with the pSB1c-aroG<sup>fbr</sup>-tktA-pheA plasmid into
+									<i>E.
+										coli</i>
+									BWΔCD,
+									induced them in the ZYM5052
+									medium, and
+									transferred them into M9 medium containing 20 g/L glucose for fermentation.
+									After 24 h of cultivation, we
+									performed HPLC
+									analysis to test their HPP production. Especially, when <i>tyrR</i> was
+									silenced, a
+									significant increase of HPP was
+									achieved
+									with an improvement of 113.6% (0.704 g/L) compared to the strains only
+									expressing the enhanced upstream
+									pathways. We
+									selected a non-mutant <i>tyrRi</i> strain for flask fermentation, and the HPP
+									titer
+									reached 0.91 g/L (Fig. 8).
+								</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/图片7.tif" alt="">
 								</div>
-							
-							
-								<div class="figure-container" style="width: 90%;margin: 0 auto;"">
-										<img src=" ../../static/result/fig6.png" alt="">
+								<p><b>Figure 8.</b>Bar graph of HPP production with different genes inhibited by
+									CRISPRi. The blue column represents the strain transformed
+									by pATP, the green column is for the strain transformed by pATP and
+									R6K-dCas9-sgRNA, and the orange columns indicate the
+									strain transformed by pATP and R6K-dCas9-sgRNA mutants. The control group was
+									the BWΔCD strain carrying no plasmid.</p>
+							</div>
+							<div id="slide5-chapter1" style="margin-bottom:10%;">
+								<h2>Evaluation of Metabolic Engineering and Directed Evolution</h2>
+								<p>The optimized clones (gY9s-HmaSV152G-Bio177) obtained from the screening were
+									transformed into the bacterial host (pATP
+									or tyrRi). The experiment groups were listed in the Table 1. After
+									cultivation
+									and
+									induced protein expression, the
+									bacteria were transferred to a fermentation medium using glucose as the
+									substrate
+									and fermented in a shake flask at 30°C
+									for 8 h.</p>
+								<p>Table 1. List of plasmids used to generate different strains in each group
+									for
+									fermentation.</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/12.jpg" alt="">
 								</div>
-								
-								
-								<div class="figure-container" style="width: 95%;margin: 0 auto;"">
-										<img src=" ../../static/result/fig7.png" alt="">
+								<p>Compared HMA1, HMA3 and HMA5 clones, we found that gene overexpression or
+									silencing
+									alone had limited effects on overall
+									fermentation promotion. However, when two approaches are combined, it
+									allowed
+									the
+									endogenous HPP synthesis pathway to
+									achieve balanced, stable and sustained expression, lead to a remarkable
+									increase
+									in
+									the fermentation yield.</p>
+								<p>Contrasted the HMA1 and HMA2, HMA3 and HMA4, HMA5 and HMA6 pairs, we found
+									that
+									the
+									essential limiting factor was the
+									enzymatic activity of hydroxymandelate synthase, which significantly
+									restricted
+									HMA
+									production (Fig. 9).</p>
+
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/11.jpg" alt="">
 								</div>
-								
-								<div class="figure-container" style="width: 60%;margin: 0 auto;"">
-										<img src=" ../../static/result/fig8.png" alt="">
+								<p>Fermentation was carried out for a long time using the HMA5 and HMA6 clones.
+									Aliquots
+									were collected every two hours,
+									compared with HmaSWT, the HmaSV152G obtained through the screening, showed a
+									4.73-fold increase in HMA production and
+									produced 3.63 g/L HMA after 24 h with a single supply of 20 g/L glucose
+									(Fig.
+									10).
+								</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/t9.jpg" alt="">
 								</div>
-							
-								<div class="figure-container" style="width: 60%; margin: 0 auto;">
-									<img src="../../static/result/fig9.png" alt="">
+								<p><b>Figure 9.</b>Bar graph to compare relative HMA levels produced by different
+									strains. Solid black dots indicate the presence of the
+									plasmids, hollow black dots indicate their absence.
+								</p>
+								<div class="figure-container" style="width: 60%;margin: 0 auto;">
+									<img src="../../images/图片7.tif" alt="">
 								</div>
-								
+								<p><b>Figure 10.</b>Comparison of HMA production by the HMA5 and HMA6 strains. The
+									bacteria were fermented in shaking flasks for 24 h with a
+									single supply of 20 g/L glucose as the substrate, and HMA levels monitored at
+									indicated time points</p>
+								</p>
 							</div>
 						</div>
 					</div>
-				</section>
 			</div>
+			</section>
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 	</div>
+	</div>
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 		<p style="font-size: 20px;">TOP</p>
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@@ -320,7 +564,7 @@ <h3 class="c-footer__heading">Contact info</h3>
 		<div class="c-corporate-footer">
 			<div class="u-container">
 				<img src="../../static/logo.png" width="120px" height="40px">
-				<p class="c-corporate-footer__legal">iDEC-2023 NEFU_China</p>
+				<p class="c-corporate-footer__legal">iDEC-2022 NEFU_China</p>
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@@ -338,4 +582,4 @@ <h3 class="c-footer__heading">Contact info</h3>
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