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 |