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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 10(63), p. 870-873, 2007

DOI: 10.1107/s1744309107043217

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Expression, purification, crystallization and preliminary X-ray crystallographic analysis of a resuscitation-promoting factor fromMycobacterium tuberculosis

Journal article published in 2007 by Alessia Ruggiero, Barbara Tizzano, Arie Geerlof, Emilia Pedone, Carlo Pedone, Matthias Wilmanns ORCID, Rita Berisio ORCID
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This paper is available in a repository.

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Abstract

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 I422, with unit-cell parameters a = 97.63, b = 97.63, c = 114.87 A. Diffraction data have also been collected from a selenomethionine derivative at 2.9 A resolution. Model building using the phases derived from the multiwavelength anomalous dispersion experiment is in progress.