5ZRT
Crystal structure of human C1ORF123 protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-10-10 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.9797 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.320, 65.350, 95.050 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.900 - 1.900 |
R-factor | 0.1778 |
Rwork | 0.175 |
R-free | 0.22030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1zso |
RMSD bond length | 0.021 |
RMSD bond angle | 2.037 |
Data reduction software | MOSFLM |
Data scaling software | Aimless |
Phasing software | BALBES |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.900 | 1.940 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.060 | |
Number of reflections | 29180 | 10058 |
<I/σ(I)> | 13.8 | 3 |
Completeness [%] | 98.1 | 97.2 |
Redundancy | 5.5 | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 293 | 0.2M magnesium chloride hexahydrate, 0.1M sodium citrate tribasic buffer pH 6.5, 20% polyethylene glycol 3350 |