5CH3
E3 alpha-esterase-7 carboxylesterase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-20 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9393 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 48.574, 100.472, 221.715 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.760 - 1.710 |
R-factor | 0.17292 |
Rwork | 0.171 |
R-free | 0.21426 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4fng |
RMSD bond length | 0.019 |
RMSD bond angle | 1.841 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.800 | 1.740 |
High resolution limit [Å] | 1.710 | 1.710 |
Rmerge | 0.145 | 3.800 |
Number of reflections | 56138 | |
<I/σ(I)> | 19.5 | 1.1 |
Completeness [%] | 99.9 | 98.6 |
Redundancy | 29 | 28.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 20% PEG 2K MME, 100mM sodium acetate pH 4.5 |