Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9765 |
| Spacegroup name | P 2 2 21 |
| Unit cell lengths | 176.520, 179.200, 389.690 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.470 - 4.300 |
| R-factor | 0.2028 |
| Rwork | 0.202 |
| R-free | 0.25720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.975 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.470 | 4.430 |
| High resolution limit [Å] | 4.300 | 4.300 |
| Number of reflections | 79835 | 6842 |
| <I/σ(I)> | 10.9 | 3.1 |
| Completeness [%] | 94.2 | |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 277 | Crystals were grown at in vapour diffusion experiments by mixing equal volumes of protein with a reservoir solution containing 1.1 to 1.3 M sodium malonate, pH 7.4 |






