4RE6
Acylaminoacyl peptidase complexed with a chloromethylketone inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-22 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9334 |
Spacegroup name | P 1 |
Unit cell lengths | 71.580, 97.300, 99.160 |
Unit cell angles | 105.15, 103.96, 100.26 |
Refinement procedure
Resolution | 19.850 - 2.550 |
R-factor | 0.21398 |
Rwork | 0.212 |
R-free | 0.25963 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 3o4h |
RMSD bond length | 0.011 |
RMSD bond angle | 1.470 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 20.000 | 20.000 | 2.620 |
High resolution limit [Å] | 2.550 | 11.400 | 2.550 |
Rmerge | 0.071 | 0.022 | 0.505 |
Number of reflections | 68281 | ||
<I/σ(I)> | 13.38 | 39.03 | 2.16 |
Completeness [%] | 86.4 | 79.2 | 51.1 |
Redundancy | 2.18 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 78 mM sodium acetate buffer, 2.2% w/v PEG Mw4000, 5.2 mM dithiothreitol, 0.34 mM EDTA. Protein crystals were soaked in the inhibitor solution., pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |