8UN9
Crystal structure of the MrfB exonuclease catalytic core
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 289 |
Detector technology | PIXEL |
Collection date | 2023-02-07 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 1.127129 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 72.874, 37.928, 92.616 |
Unit cell angles | 90.00, 99.15, 90.00 |
Refinement procedure
Resolution | 41.740 - 2.103 |
Rwork | 0.175 |
R-free | 0.23250 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.301 |
Data reduction software | DIALS |
Data scaling software | DIALS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.720 | 2.160 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.064 | 0.489 |
Rmeas | 0.076 | 0.576 |
Rpim | 0.040 | 0.303 |
Number of reflections | 29515 | 2294 |
<I/σ(I)> | 14.2 | 2.7 |
Completeness [%] | 99.6 | 97.7 |
Redundancy | 6.5 | 6.7 |
CC(1/2) | 0.998 | 0.917 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 289 | The MrfB catalytic core (33-279) was crystallized by hanging drop with 1 microliter of 10 mg/mL protein (in 25 mM Tris pH 7.5, 125 mM NaCl, 1 mM TCEP, 5 mM MgCl2, 2 mM dTMP) and 1 microliter of well solution (0.1 M HEPES pH 7.5, 15% PEG Smear medium, 8% ethylene glycol). Crystals were harvested in 20 mM Tris pH 7.5, 125 mM NaCl, 1 mM TCEP, 5 mM MgCl2, 2 mM dTMP, 0.1 M HEPES pH 7.5, 20% PEG smear medium, and cryoprotected with the addition of 25% ethylene glycol |