1E5T
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-07-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 70.700, 99.700, 110.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 21.000 - 1.700 |
| R-factor | 0.184 |
| Rwork | 0.184 |
| R-free | 0.20600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qfm |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.000 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.851) |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 21.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.400 |
| Rmerge | 0.061 * | 0.538 * |
| Total number of observations | 281721 * | |
| Number of reflections | 82125 | |
| <I/σ(I)> | 16.3 | 1.6 |
| Completeness [%] | 94.6 | 85.6 |
| Redundancy | 3.4 | 3.01 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 | 4 * | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | mPEG5000 | 17 (%(w/v)) | |
| 3 | 1 | reservoir | glycerol | 15 (%(v/v)) | |
| 4 | 1 | reservoir | monothioglyycerol | 1 (%(v/v)) | |
| 5 | 1 | reservoir | 20 (mM) | ||
| 6 | 1 | reservoir | TRIS | 100 (mM) |
