Protomeric substructure from an octameric assembly of M. tuberculosis RNA polymerase in complex with sigma-b initiation factor

Structural basis of the mycobacterial stress-response RNA polymerase auto-inhibition via oligomerization

M. tuberculosis RNA polymerase in complex with sigma-b initiation factor

Movie frames were aligned, dose-weighted, binned by two and averaged using Motioncor2 (Zheng S.Q Nat. Methods. 2017; 14: 331-332). Movie sums were used for contrast transfer function (CTF) estimation with Gctf (Zhang K. J. Struct. Biol. 2016; 193: 1-12)

DNA-directed RNA polymerase subunit alpha

DNA-directed RNA polymerase subunit beta

DNA-directed RNA polymerase subunit beta'

DNA-directed RNA polymerase subunit omega

RNAP subunit alpha,RNA polymerase subunit alpha,Transcriptase subunit alpha

RNAP subunit beta,RNA polymerase subunit beta,Transcriptase subunit beta

RNAP subunit beta',RNA polymerase subunit beta',Transcriptase subunit beta'

RNAP omega subunit,RNA polymerase omega subunit,Transcriptase subunit omega

French Infrastructure for Integrated Structural Biology (FRISBI)

M. tuberculosis RNA polymerase in complex with sigma-b initiation factor: (alpha)2-beta-beta'-omega-sigB protomeric substructure from an octameric assembly of protomers.

RNA polymerase, self-assembly, octamer, tuberculosis, stress response, hibernation, TRANSCRIPTION