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Expression, purification and crystallization of phosphoribosyl transferase from a mycobacteriophage
Author(s) -
Li Lei,
Lee Eungyu,
Shaw Neil
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18002480
Subject(s) - transferase , biology , mutant , crystallization , microbiology and biotechnology , virology , mycobacterium tuberculosis , tuberculosis , enzyme , chemistry , biochemistry , medicine , gene , organic chemistry , pathology
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 C 222 1 , 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.