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Cloning, expression, purification, crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Mycobacterium tuberculosis

Journal Article · · Acta Crystallographica. Section F
 [1];  [2];  [1]; ;  [2]
  1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012 (India)
  2. Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560 012 (India)
The peptidyl-tRNA hydrolase from M. tuberculosis has been crystallized in three closely related forms, two orthorhombic and one monoclinic, and X-ray diffraction data have been collected from them. Peptidyl-tRNA hydrolase catalyses the cleavage of the ester link between the peptide and the tRNA in peptidyl-tRNAs that, for various reasons, have dropped off the translating ribosomes. This enzyme from Mycobacterium tuberculosis has been crystallized in three related but distinct forms: P2{sub 1}2{sub 1}2{sub 1}, unit-cell parameters a = 36.30, b = 61.85, c = 73.97 Å, P2{sub 1}, a = 35.83, b = 73.79, c = 59.79 Å, β = 92.3°, and P2{sub 1}2{sub 1}2{sub 1}, a = 35.84, b = 57.06, c = 72.59 Å. X-ray data have been collected from all three forms.
OSTI ID:
22356433
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 9 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English