Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 28, Issue 20, Pages -Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2020.115662
Keywords
Seryl-tRNA synthetase; E. coli orthogonality; Genetic code expansion; X-ray crystallography; Non-canonical amino acids
Funding
- NIH [R01 GM062159]
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We report the development of the orthogonal amber-suppressor pair Archaeoglobus fulgidus seryl-tRNA (Af-tRNA(Ser))/Methanosarcina mazei seryl-tRNA synthetase (MmSerRS) in Escherichia coli. Furthermore, the crystal structure of MmSerRS was solved at 1.45 angstrom resolution, which should enable structure-guided engineering of its active site to genetically encode small, polar noncanonical amino acids (ncAAs).
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