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Crystallization and preliminary crystallographic analysis of the putative sugar‐binding protein Msmeg_0515 (AgaE) from Mycobacterium smegmatis
Author(s) -
Almourfi Feras M.,
Rodgers H. Fiona,
Sedelnikova Svetlana E.,
Baker Patrick J.
Publication year - 2015
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/s2053230x15000035
Subject(s) - mycobacterium smegmatis , crystallography , crystallization , chemistry , resolution (logic) , escherichia coli , gene , biology , biochemistry , mycobacterium tuberculosis , medicine , tuberculosis , organic chemistry , pathology , artificial intelligence , computer science
Msmeg_0515 , a gene from Mycobacterium smegmatis strain 155 encoding the ligand‐binding domain, AgaE, of a putative ABC sugar transporter system, has been cloned into a pET‐28a vector system, overexpressed in Escherichia coli and purified. The truncated protein lacking the first 27 residues, which correspond to a N‐terminal signal sequence, was crystallized using the sitting‐drop vapour‐diffusion technique. The crystals of this protein diffracted to 1.48 Å resolution and belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 64.06, b = 69.26, c = 100.74 Å, α = β = γ = 90° and with one molecule in the asymmetric unit.