Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM16 |
Synchrotron site | ESRF |
Beamline | BM16 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-11-17 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 107.727, 130.165, 126.726 |
Unit cell angles | 90.00, 93.61, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.650 |
R-factor | 0.168 |
Rwork | 0.167 |
R-free | 0.19200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ewo |
RMSD bond length | 0.015 |
RMSD bond angle | 1.507 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.360 | 1.740 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.080 | 0.440 |
Number of reflections | 417377 | |
<I/σ(I)> | 8.4 | 2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 3.7 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 1.5M SODIUM CHLORIDE, 1.6M AMMONIUM SULFATE, 0.1M HEPES PH 7.5, 5MM AGMATINE |