5E4Y
Orthorhombic structure of the acetyl esterase MekB
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-02-04 |
Detector | DECTRIS PILATUS 2M |
Wavelength(s) | 0.8729 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 58.346, 79.946, 142.177 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.736 - 2.800 |
R-factor | 0.1885 |
Rwork | 0.186 |
R-free | 0.23670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5d60 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.490 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.740 | 2.950 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.083 | |
Number of reflections | 16961 | |
<I/σ(I)> | 6.01 | 2.6 |
Completeness [%] | 99.7 | 99.9 |
Redundancy | 5.9 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.1 M MES pH 6, 5 % PEG 1000, 30 % PEG 600, 10 % Glycerol |