<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>47</viewCount><searchCount>0</searchCount></scores><additional><submitter>Li L</submitter><funding>The National Natural Science Foundation of China</funding><pagination>161-165</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5947702</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>74(Pt 3)</volume><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&lt;sub>1&lt;/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.</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology communications</journal><pubmed_title>Expression, purification and crystallization of phosphoribosyl transferase from a mycobacteriophage.</pubmed_title><pmcid>PMC5947702</pmcid><funding_grant_id>31100877</funding_grant_id><funding_grant_id>31000332</funding_grant_id><funding_grant_id>31100208</funding_grant_id><funding_grant_id>31170782</funding_grant_id><funding_grant_id>31110103915</funding_grant_id><pubmed_authors>Shaw N</pubmed_authors><pubmed_authors>Li L</pubmed_authors><pubmed_authors>Lee E</pubmed_authors><view_count>47</view_count></additional><is_claimable>false</is_claimable><name>Expression, purification and crystallization of phosphoribosyl transferase from a mycobacteriophage.</name><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&lt;sub>1&lt;/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.</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Mar</publication><modification>2024-12-03T22:50:54.056Z</modification><creation>2020-05-22T11:35:07Z</creation></dates><accession>S-EPMC5947702</accession><cross_references><pubmed>29497020</pubmed><doi>10.1107/S2053230X18002480</doi><doi>10.1107/s2053230x18002480</doi></cross_references></HashMap>