Publication Date:
2015-01-01
Description:
Rv3899c, a hypothetical protein fromMycobacterium tuberculosisthat is conserved within the mycobacteria, is predicted to be secreted and has been found in culture filtrates. Here, Rv3899c has been cloned, expressed inEscherichia coliand purified using standard chromatographic techniques. The hanging-drop vapour-diffusion method with PEG 3350 as a precipitant was used to crystallize the protein. N-terminal sequencing results showed that the amino-acid sequence of the crystallized protein began with GATAG, indicating that it is a fragment containing residues 184–410 of Rv3899c. Rv3899c184–410crystals exhibited the symmetry of space groupP212121, with unit-cell parametersa= 49.88,b= 54.72,c= 75.52 Å, α = β = γ = 90°, and diffracted to a resolution of 1.90 Å.
Electronic ISSN:
2053-230X
Topics:
Biology
,
Chemistry and Pharmacology
,
Geosciences
,
Physics
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