Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Stephen R. Ashford"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1432:413-418
The gene for DNA ligase (EC 6.5.1.2) from thermophilic bacterium Bacillus stearothermophilus NCA1503 has been cloned and the complete nucleotide sequence determined. The ligase gene encodes a protein 670 amino acids in length. The gene was overexpres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::beafa92279811891132107d6f6f78b36
https://doi.org/10.1016/s0167-4838(99)00122-3
https://doi.org/10.1016/s0167-4838(99)00122-3
Publikováno v:
Journal of Biological Chemistry. 271:11083-11089
The bacteriophage T7 DNA ligase gene was amplified using polymerase chain reaction-based methods and cloned into a T7 promoter-based expression vector. The protein was overexpressed to greater than 15% of total soluble protein and purified to homogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3ffd4a8564eb64ddb28f7652a2ab4106
https://doi.org/10.1074/jbc.271.19.11083
https://doi.org/10.1074/jbc.271.19.11083
Publikováno v:
Nucleic acids research. 24(12)
Treatment of T7 DNA ligase with a range of proteases generates two major fragments which are resistant to further digestion. These fragments, of molecular weight 16 and 26 kDa, are derived from the N- and C-termini of the protein, respectively. The p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f96c52f7ef902cecc9e4b774194f38f3
https://pubmed.ncbi.nlm.nih.gov/8710497
https://pubmed.ncbi.nlm.nih.gov/8710497
Publikováno v:
Cell. 85(4)
The crystal structure of the ATP-dependent DNA ligase from bacteriophage T7 has been solved at 2.6 Å resolution. The protein comprises two domains with a deep cleft running between them. The structure of a complex with ATP reveals that the nucleotid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5757293d537315707d43e68357f4e492
https://pubmed.ncbi.nlm.nih.gov/8653795
https://pubmed.ncbi.nlm.nih.gov/8653795
Publikováno v:
Nucleic acids research. 23(11)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0941eaf448ef178e378edb0a60fb4283
https://pubmed.ncbi.nlm.nih.gov/7596839
https://pubmed.ncbi.nlm.nih.gov/7596839
Autor:
Fiona H. Rodgers, David W. Rice, Timothy J. Stillman, Stephen R. Ashford, Patrick J. Baker, Ronald L. Hanson, Andrew P. Turnbull
Publikováno v:
Journal of molecular biology. 236(2)
The NAD(+)-dependent leucine dehydrogenase from Bacillus sphaericus has been crystallized by the hanging drop method of vapour diffusion, using ammonium sulphate as the precipitant. The crystals belong to the tetragonal system and are in space group
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8435de70975268b58c2b9de62a92818a
https://pubmed.ncbi.nlm.nih.gov/8107149
https://pubmed.ncbi.nlm.nih.gov/8107149