1W7V
ZnMg substituted aminopeptidase P from E. coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-07-01 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 111.731, 236.527, 137.997 |
| Unit cell angles | 90.00, 106.34, 90.00 |
Refinement procedure
| Resolution | 37.800 - 2.000 |
| R-factor | 0.157 |
| Rwork | 0.156 |
| R-free | 0.18000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1WL9 WITH ALL HET ATOMS WATERS AND MULTIPLE CONFORMERS REMOVED |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.106 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.070 | 0.440 |
| Number of reflections | 225729 | |
| <I/σ(I)> | 13.9 | 6 |
| Completeness [%] | 97.9 | 96.3 |
| Redundancy | 2.9 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.3 | ROOM TEMPERATURE HANGING DROP WITH 16% PEG4K, 0.1 M TRIS (PH8.3), 0.2 M MGCL2. TRANSFERRED TO A DROP ABOVE CONDITIONS PLUS WITH 10 MM VAL-PRO-LEU PEPTIDE AND ALLOWED TO EQUILIBRATE OVERNIGHT., pH 8.30 |
