BBa_J70459
BBa_J70459 Version 1 (Component)
yfp RBS, {0,5;15,10} family member - B0031 simulator (reverse oligo)

BBa_K1497197
BBa_K1497197 Version 1 (Component)
B0034-CHI - Chalcone Isomerase from Petunia with strong RBS

BBa_K228815
BBa_K228815 Version 1 (Component)
Promoter(constitutive)+RBS(B0034)+lacI(C0012)+terminator(B0015)

Adapter Bi
BBa_K1807015 Version 1 (Component)
This device allows for the IPTG-inducible expression of lacZα peptide which in the presence of

BBa_K855007
BBa_K855007 Version 1 (Component)
LuxR generator regulated by Lac Promoter followed plux promoter (R0062) and RBS (B0034)

BBa_J06551
BBa_J06551 Version 1 (Component)
Construction intermediate: lambda cI with RBS and hybrid LacI promoter (R0011.B0034.C0051)

iGEM Parts Registry
igem_collection Version 1 (Collection)
The iGEM Registry is a growing collection of genetic parts that can be mixed and matched to build synthetic biology devices and systems. As part of the synthetic biology community's efforts to make biology easier to engineer, it provides a source of genetic parts to iGEM teams and academic labs.

Intein_assisted_Bisection_Mapping
Intein_assisted_Bisection_Mapping_collection Version 1 (Collection)
Split inteins are powerful tools for seamless ligation of synthetic split proteins. Yet, their use remains limited because the already intricate split site identification problem is often complicated by the requirement of extein junction sequences. To address this, we augmented a mini-Mu transposon-based screening approach and devised the intein-assisted bisection mapping (IBM) method. IBM robustly revealed clusters of split sites on five proteins, converting them into AND or NAND logic gates. We further showed that the use of inteins expands functional sequence space for splitting a protein. We also demonstrated the utility of our approach over rational inference of split sites from secondary structure alignment of homologous proteins. Furthermore, the intein inserted at an identified site could be engineered by the transposon again to become partially chemically inducible, and to some extent enabled post-translational tuning on host protein function. Our work offers a generalizable and systematic route towards creating split protein-intein fusions and conditional inteins for protein activity control.