{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":47,"searchCount":0},"additional":{"submitter":["Li L"],"funding":["The National Natural Science Foundation of China"],"pagination":["161-165"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5947702"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["74(Pt 3)"],"pubmed_abstract":["Tuberculosis (TB) continues to remain a leading cause of death globally. Of particular concern is the emergence and rise in incidence of multidrug-resistant and extremely drug-resistant cases of TB. To counter this threat, it is important to explore alternative therapies, including phage therapy. Phage BTCU-1 specifically infects Mycobacterium spp. and kills the majority of them. Intriguingly, many proteins from the phage do not share high amino-acid sequence identity with proteins from species other than phages. Here, the expression, purification and crystallization of one such protein, a putative phosphoribosyl transferase from phage BTCU-1, is reported. The crystals belonged to space group C222<sub>1</sub>, with unit-cell parameters a = 59.71, b = 64.42, c = 65.32 Å, α = β = γ = 90°. The crystals diffracted X-rays to 2.2 Å resolution."],"journal":["Acta crystallographica. Section F, Structural biology communications"],"pubmed_title":["Expression, purification and crystallization of phosphoribosyl transferase from a mycobacteriophage."],"pmcid":["PMC5947702"],"funding_grant_id":["31100877","31000332","31100208","31170782","31110103915"],"pubmed_authors":["Shaw N","Li L","Lee E"],"view_count":["47"],"additional_accession":[]},"is_claimable":false,"name":"Expression, purification and crystallization of phosphoribosyl transferase from a mycobacteriophage.","description":"Tuberculosis (TB) continues to remain a leading cause of death globally. Of particular concern is the emergence and rise in incidence of multidrug-resistant and extremely drug-resistant cases of TB. To counter this threat, it is important to explore alternative therapies, including phage therapy. Phage BTCU-1 specifically infects Mycobacterium spp. and kills the majority of them. Intriguingly, many proteins from the phage do not share high amino-acid sequence identity with proteins from species other than phages. Here, the expression, purification and crystallization of one such protein, a putative phosphoribosyl transferase from phage BTCU-1, is reported. The crystals belonged to space group C222<sub>1</sub>, with unit-cell parameters a = 59.71, b = 64.42, c = 65.32 Å, α = β = γ = 90°. The crystals diffracted X-rays to 2.2 Å resolution.","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Mar","modification":"2024-12-03T22:50:54.056Z","creation":"2020-05-22T11:35:07Z"},"accession":"S-EPMC5947702","cross_references":{"pubmed":["29497020"],"doi":["10.1107/S2053230X18002480","10.1107/s2053230x18002480"]}}