Part:BBa_K325219:ArabinosetoLight
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Description
This page describes the relationship between Arabinose concentration in the medium with light output. We used a [http://www.bmglabtech.com/products/microplate-reader/instruments.cfm?product_id=2 FLUOstar OPTIMA] microplate reader to quantify the light output. Protocol and plate reader settings used are given below.
Data
Performance
Experiment1 | Characteristic1 | Value1 |
---|---|---|
Transfer Function | Maximum Output | 6.6 PoPS cell-1 |
Hill coefficient | 1.6 | |
Switch Point | 1.5E-9 M 3OC6HSL, exogenous | |
Response time: | <1 min | |
Input compatibility | Strong response to | 3OC6HSL, C6HSL , C7HSL, 3OC8HSL, C8HSL |
Weak response to | C4HSL, C10HSL, C12HSL | |
Stability | Genetic Stability (Low/High Input) |
>92/>56 generations |
Performance Stability (Low/High Input) |
>92/>56 generations | |
Demand | Internal Demand (Low/High Input) |
Not measured |
Transcriptional output demand: (Low/High Input) Nt = length of downstream transcript in nucleotides |
(0/6xNt) nucleotides cell-1 s-1 | |
(0/1.5E-1xNt) RNAP cell-1 | ||
Growth Rate (Low/High Input) |
54/59 min Doubling time |
1Measured by the [http://2010.igem.org/Team:Cambridge Cambridge iGEM team 2010]
Compatibility
Chassis: Device has been shown to work in Top 10 (Invitrogen)
Plasmids: Device has been shown to work on pSB1C3
References
[http://www.ncbi.nlm.nih.gov/pubmed/18949818 [1]:] S.M. Marques and J.C.G. Esteves da Silva, (2009) Firefly Bioluminescence: A Mechanistic Approach of Luciferase Catalyzed Reactions,Life 61, 6-17.
[http://www.nature.com/nature/journal/v440/n7082/abs/nature04542.html [2]:] T. Nakatsu et al. (2006) Structural Basis for the spectral difference in luciferase bioluminescence, Nature 440(16), 372-376.
[http://www.ncbi.nlm.nih.gov/pubmed/11457857 [3]:] K. Gomi and N. Kajiyama, (2001) Oxyluciferin, a Luminescence Product of Firefly Luciferase, Is Enzymatically Regenerated into Luciferin, The Journal of Biological Chemistry, 276(39), 36508-36513.