6HQ7
Structure of EAL Enzyme Bd1971 - cGMP bound form
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 | 2013-10-05 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 31 |
| Unit cell lengths | 82.570, 82.570, 134.590 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 63.150 - 2.460 |
| R-factor | 0.2229 |
| Rwork | 0.221 |
| R-free | 0.25300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | used full length model |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.480 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.1.29) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 63.150 | 63.150 | 2.520 |
| High resolution limit [Å] | 2.460 | 11.000 | 2.460 |
| Rmerge | 0.043 | 0.037 | 0.594 |
| Rmeas | 0.048 | 0.041 | 0.658 |
| Rpim | 0.021 | 0.018 | 0.282 |
| Total number of observations | 192538 | ||
| Number of reflections | 37250 | 421 | 2752 |
| <I/σ(I)> | 18.9 | ||
| Completeness [%] | 99.9 | 98.4 | 100 |
| Redundancy | 5.2 | 5 | 5.4 |
| CC(1/2) | 0.999 | 0.997 | 0.783 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.7 | 291 | 0.2M Mg Formate pH 5.7 20% w/v PEG 3350 2.5 mM cGMP |
