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Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of a resuscitation‐promoting factor from Mycobacterium tuberculosis
Author(s) -
Ruggiero Alessia,
Tizzano Barbara,
Geerlof Arie,
Pedone Emilia,
Pedone Carlo,
Wilmanns Matthias,
Berisio Rita
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107043217
Subject(s) - crystallization , resuscitation , mycobacterium tuberculosis , materials science , crystallography , tuberculosis , chemistry , medicine , organic chemistry , surgery , pathology
The resuscitation‐promoting factor RpfB, the most complex of the five resuscitation‐promoting factors produced by M. tuberculosis , is devoted to bacterial reactivation from the dormant state. RpfB consists of 362 residues predicted to form five domains. An RpfB fragment containing the protein catalytic domain and a G5 domain has been successfully crystallized using vapour‐diffusion methods. This is the first crystallographic study of a resuscitation‐promoting factor. Crystals of this protein belong to space group I 422, with unit‐cell parameters a = 97.63, b = 97.63, c = 114.87 Å. Diffraction data have also been collected from a selenomethionine derivative at 2.9 Å resolution. Model building using the phases derived from the multiwavelength anomalous dispersion experiment is in progress.

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