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 d min of 3.15 Å. The collected data revealed preliminary structural information regarding this newly discovered protein.
| Original language | English |
|---|---|
| Pages (from-to) | 604-608 |
| Number of pages | 5 |
| Journal | Acta Crystallographica Section F:Structural Biology Communications |
| Volume | 76 |
| DOIs | |
| State | Published - 1 Dec 2020 |
Bibliographical note
Publisher Copyright:© 2020 International Union of Crystallography. All rights reserved.
Keywords
- ATP-dependent RNA helicases
- DEAD-box proteins
- Helicase C domain
- Protozoan proteins
- Trypanosoma brucei
- ZC3H41