4OZS
RNA binding protein
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-07-05 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.980, 0.954 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.025, 75.023, 85.117 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 56.280 - 2.170 |
R-factor | 0.21933 |
Rwork | 0.217 |
R-free | 0.26549 |
RMSD bond length | 0.021 |
RMSD bond angle | 2.442 |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 56.280 | 2.250 |
High resolution limit [Å] | 2.170 | 2.170 |
Rmerge | 0.019 | 0.313 |
Number of reflections | 18791 | |
<I/σ(I)> | 24.44 | 2.68 |
Completeness [%] | 99.8 | 98.43 |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 3.35 | 293 | Diffraction quality crystals grew from 3 uL drops in 24-well sitting drop Cryschem plates (Hampton Research) in 2:1 ratios of crystallant 100 mM Sodium citrate pH 3.35, 8 % (w/v) PEG 3350 and protein equilibrated against 1 mL of crystallant at 293 K. |