6HQ2
Structure of EAL Enzyme Bd1971 - apo 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 | P 43 21 2 |
| Unit cell lengths | 92.470, 92.470, 74.120 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 74.120 - 2.450 |
| R-factor | 0.2109 |
| Rwork | 0.209 |
| R-free | 0.24900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | full length protein |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.762 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.3.11) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 74.120 | 74.120 | 2.510 |
| High resolution limit [Å] | 2.450 | 10.960 | 2.450 |
| Rmerge | 0.054 | 0.042 | 1.806 |
| Rmeas | 0.056 | 0.045 | 1.888 |
| Rpim | 0.016 | 0.014 | 0.544 |
| Total number of observations | 153929 | ||
| Number of reflections | 12284 | 177 | 886 |
| <I/σ(I)> | 23.9 | ||
| Completeness [%] | 99.5 | 98.7 | 99.4 |
| Redundancy | 12.5 | 9.4 | 12 |
| CC(1/2) | 1.000 | 1.000 | 0.815 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 291 | 0.1M Na Hepes pH 7 18% w/v PEG 12000 |
