9H4A
Ribonuclease-three Like 4 crystallization and structure determination at room temperature in the CrystalChip
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM07 |
Synchrotron site | ESRF |
Beamline | BM07 |
Temperature [K] | 293 |
Detector technology | PIXEL |
Collection date | 2024-07-16 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9795 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 48.130, 101.530, 134.030 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.470 - 2.800 |
R-factor | 0.2157 |
Rwork | 0.214 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.001 |
RMSD bond angle | 0.314 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.870 |
High resolution limit [Å] | 2.800 | 2.800 |
Number of reflections | 64222 | 3046 |
<I/σ(I)> | 4.4 | |
Completeness [%] | 92.5 | |
Redundancy | 8.23 | |
CC(1/2) | 0.974 | 0.303 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | COUNTER-DIFFUSION | 293 | Protein crystallized by counter-diffusion in the CrystalChip, stock solution at 4 mg/mL, in a reservoir containing 14% (w/v) PEG 3350, 50 mM Bis-TRIS-HCl at pH 6.5 to 7.0 |