PropertyValue
?:abstract
  • A fragment of the Trypanosoma brucei ZC3H41 protein encompassing the ATP-dependent RNA helicase domain was successfully subcloned for expression in a bacterial system (Escherichia coli). Following expression, the protein was purified and crystallized using the vapor-diffusion method. The protein crystals were optimized at a 1:1 protein:reservoir solution ratio using PPGBA 2000. The optimized crystals diffracted to a dmin of 3.15†Å. The collected data revealed preliminary structural information regarding this newly discovered protein.
is ?:annotates of
?:creator
?:journal
  • Acta_Crystallogr_F_Struct_Biol_Commun
?:license
  • unk
?:publication_isRelatedTo_Disease
?:source
  • WHO
?:title
  • ATP-dependent RNA helicase domain of the ZC3H41 protein from Trypanosoma brucei: expression, purification and crystallization
?:type
?:who_covidence_id
  • #33263572
?:year
  • 2020

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