2V3Z
Glu383Ala Escherichia coli aminopeptidase P in complex with substrate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-22 |
Detector | ADSC CCD |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 177.695, 177.695, 96.433 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.660 - 1.560 |
R-factor | 0.14 |
Rwork | 0.140 |
R-free | 0.15000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wl9 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.348 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | REFMAC |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.620 |
High resolution limit [Å] | 1.560 | 1.560 |
Rmerge | 0.070 | 0.580 |
Number of reflections | 125677 | |
<I/σ(I)> | 32.5 | 4.3 |
Completeness [%] | 99.4 | 99.8 |
Redundancy | 11 | 10 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277 | CRYSTALLISED IN 30% PEG 4K, 0.1 M TRIS PH 8.8 AT 277K. SOAKED IN 30% PEG 4K, 0.1 M TRIS PH 8.5, 1 MM MNCL2, 5 MM VAL-PRO-LEU, 10% MPD FOR 30 MIN AT 277K IMMEDIATELY PRIOR TO DATA COLLECTION. |