2IVN
Structure of UP1 protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 61.933, 69.868, 75.723 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.650 |
R-factor | 0.213 |
Rwork | 0.212 |
R-free | 0.22400 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.987 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.690 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.060 | 0.510 |
Number of reflections | 41853 | |
<I/σ(I)> | 25.1 | 2.8 |
Completeness [%] | 99.2 | 100 |
Redundancy | 4.1 | 2.84 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.6 | 25% PEG 4000, 0.3M KCL, 0.1M SODIUM CITRATE PH5.6 |