Abstract
The backbone resonance assignments of an engineered splicing-inactive mini-RecA intein based on triple resonance experiments with [13C,15N]-labeled protein are reported. The construct contains inactivating mutations specifically designed to retain most catalytic residues, especially those that are potentially metal-coordinating. The assignments are essential for protein structure determination of a precursor with an active N-terminal catalytic cysteine and for investigation of the atomic details of splicing.
| Original language | English |
|---|---|
| Pages (from-to) | 235-238 |
| Number of pages | 4 |
| Journal | Biomolecular NMR Assignments |
| Volume | 9 |
| Issue number | 2 |
| DOIs | |
| State | Published - Oct 22 2015 |
Keywords
- Intein
- Protein splicing
- Tuberculosis
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