The successful crystallization of the ZC3H41 protein RNA helicase domain from Trypanosoma brucei provides preliminary structural information for this newly discovered protein.
Crystallization of TbZC3H41 helicase domain achieved at 3.15 Å; leaves open its utility for future inhibitor studies.
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 d min of 3.15 Å. The collected data revealed preliminary structural information regarding this newly discovered protein.
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Izhaki-Tavor et al. (2020) studied this question.
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