deletions | additions       diff --git a/Results_Protein_production_and_baseline__.md b/Results_Protein_production_and_baseline__.md  index d7aa615..4fe5231 100644  --- a/Results_Protein_production_and_baseline__.md  +++ b/Results_Protein_production_and_baseline__.md 
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# Results   ## Protein production and baseline values   In total, 123 proteins, including native BglB, were purified with immobilized metal affinity chromatography and eluted in 200 μL HEPES buffer. Of the 123 proteins synthesized, 85 proteins express and purify as soluble protein. Greater than 65% of mutants maintained the yields obtained by native BglB while roughly 30% did not express and purify as a soluble protein above our limit of detection (0.1 mg/mL) for protein yield after purification based on A280 and SDS-PAGE. Of the 85 proteins with expression, 76 mutants displayed apredictive  melting temperature that  fit to our logistic equation. Native BglB displayed an average melting temperature of 39.6 C. [Summarize protein production specifics]  ## Thermal stability of mutants compared to wild type   The average melting temperature across Across  all 76 point mutations mutations, the average melting temperature  was 40.1 degrees C (plus or minus .88 C). C) while the average kurtosis was  The overall effect of point mutations was minimal on melting temperature, suggesting that single  point mutationsgenerally  do not illicit a strong  affect the on  protein structure. However, the The  melting temperature range of the all  point mutations was 33.8 degrees C to 45.3 degrees C, a deviation of roughly six degrees in either direction from that of wild type. ___ % displayed a melting temperature better than that of wild type. ____%'s melting temperature differed than that of wild type by two standard deviations.  [Describe what we found regarding the range of thermal stabilities we observed]