Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lucy J. Fitschen"'
Publikováno v:
Engineering Microbiology, Vol 4, Iss 1, Pp 100120- (2024)
Recombineering is an essential tool for molecular biologists, allowing for the facile and efficient manipulation of bacterial genomes directly in cells without the need for costly and laborious in vitro manipulations involving restriction enzymes. Th
Externí odkaz:
https://doaj.org/article/26db5ad3b59847bd925a78c8f3e21d7a
Autor:
Timothy P. Newing, Jodi L. Brewster, Lucy J. Fitschen, James C. Bouwer, Nikolas P. Johnston, Haibo Yu, Gökhan Tolun
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
Redβ annealase catalyses single-strand annealing homologous DNA recombination. Here, the authors present a cryo-EM structure of a Redβ annealing intermediate bound to two complementary 27mer oligonucleotides.
Externí odkaz:
https://doaj.org/article/d8eae846edef420e98dca3a781c83034
Autor:
Stefan H Mueller, Lucy J Fitschen, Afnan Shirbini, Samir M Hamdan, Lisanne M Spenkelink, Antoine M van Oijen
Publikováno v:
Nucleic acids research.
The activity of enzymes is traditionally characterised through bulk-phase biochemical methods that only report on population averages. Single-molecule methods are advantageous in elucidating kinetic and population heterogeneity but are often complica
Autor:
Timothy P, Newing, Jodi L, Brewster, Lucy J, Fitschen, James C, Bouwer, Nikolas P, Johnston, Haibo, Yu, Gökhan, Tolun
Publikováno v:
Nature communications. 13(1)
The Redβ protein of the bacteriophage λ red recombination system is a model annealase which catalyzes single-strand annealing homologous DNA recombination. Here we present the structure of a helical oligomeric annealing intermediate of Redβ, consi
Autor:
Timothy Newing, Jodi L. Brewster, Haibo Yu, Nikolas P. Johnston, Lucy J. Fitschen, Gökhan Tolun
The bacteriophage λ red recombination system catalyzes the single-strand annealing homologous DNA recombination reaction, in which Redβ annealase protein plays a critical role. Using cryogenic electron microscopy, we were able to determine a struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::671bdea2a39032f806e7c158e1a5d96d
https://doi.org/10.1101/2022.04.09.487726
https://doi.org/10.1101/2022.04.09.487726
Autor:
Stefan H. Mueller, Lucy J. Fitschen, Afnan Shirbini, Samir M. Hamdan, Lisanne M. Spenkelink, Antoine M. van Oijen
The activity of enzymes is traditionally characterised through bulk-phase biochemical methods that only report on population averages. Single-molecule methods are advantageous in elucidating kinetic and population heterogeneity but are often complica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0162df072c39cacc6ef2439afe313a62
https://doi.org/10.1101/2022.03.03.482895
https://doi.org/10.1101/2022.03.03.482895