SwePub
Sök i SwePub databas

  Extended search

Träfflista för sökning "WFRF:(Ramakrishnan P) srt2:(2005-2009)"

Search: WFRF:(Ramakrishnan P) > (2005-2009)

  • Result 1-2 of 2
Sort/group result
   
EnumerationReferenceCoverFind
1.
  •  
2.
  • Krengel, Ute, 1964, et al. (author)
  • Preliminary X-ray crystallographic analysis of the secreted chorismate mutase from Mycobacterium tuberculosis: A tricky crystallization problem solved
  • 2006
  • In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. - 1744-3091. ; 62:5, s. 441-445
  • Journal article (peer-reviewed)abstract
    • Chorismate mutase catalyzes the conversion of chorismate to prephenate in the biosynthesis of the aromatic amino acids tyrosine and phenylalanine in bacteria, fungi and plants. Here, the crystallization of the unusual secreted chorismate mutase from Mycobacterium tuberculosis (encoded by Rv1885c), a 37.2 kDa dimeric protein belonging to the AroQγ subclass of mutases, is reported. Crystal optimization was non-trivial and is discussed in detail. To obtain crystals of sufficient quality, it was critical to initiate crystallization at higher precipitant concentration and then transfer the drops to lower precipitant concentrations within 5-15 min, in an adaptation of a previously described technique [Saridakis & Chayen (2000), Protein Sci. 9, 755-757]. As a result of the optimization, diffraction improved from 3.5 to 1.3 Å resolution. The crystals belong to space group P21, with unit-cell parameters a = 42.6, b = 72.6, c = 62.0 Å., β = 104.5°. The asymmetric unit contains one biological dimer, with 167 amino acids per protomer. A soak with a transition-state analogue is also described.
  •  
Skapa referenser, mejla, bekava och länka
  • Result 1-2 of 2

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view