6HQ3
Structure of EAL Enzyme Bd1971 - halfsite-occupied 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 | 2015-01-22 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 94.580, 120.750, 56.300 |
| Unit cell angles | 90.00, 116.80, 90.00 |
Refinement procedure
| Resolution | 36.330 - 2.790 |
| R-factor | 0.2143 |
| Rwork | 0.212 |
| R-free | 0.25940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | full length protein |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.586 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.3.11) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0151) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 36.330 | 36.330 | 2.860 |
| High resolution limit [Å] | 2.790 | 12.480 | 2.790 |
| Rmerge | 0.087 | 0.036 | 0.901 |
| Rmeas | 0.105 | 0.044 | 1.131 |
| Rpim | 0.058 | 0.025 | 0.674 |
| Total number of observations | 44245 | ||
| Number of reflections | 13884 | 159 | 1031 |
| <I/σ(I)> | 8.3 | ||
| Completeness [%] | 98.5 | 94.2 | 99.3 |
| Redundancy | 3.2 | 3.1 | 2.7 |
| CC(1/2) | 0.996 | 0.998 | 0.518 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.9 | 291 | 0.2M K Nitrate pH 6.9 2.5mM cAMP 20% w/v PEG 3350 |
