1UOP
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLY-PHE-GLU-PRO
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-02-11 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 70.700, 99.300, 110.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.000 - 1.850 |
| R-factor | 0.158 |
| Rwork | 0.156 |
| R-free | 0.19400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h2z |
| RMSD bond length | 0.008 * |
| RMSD bond angle | 1.100 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.076 | 0.406 |
| Total number of observations | 247702 * | |
| Number of reflections | 66292 | |
| <I/σ(I)> | 14.6 | 2.5 |
| Completeness [%] | 98.7 | 97 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 | 4 * | Fulop, V., (1998) Cell(Cambridge,Mass.), 94, 161. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | mPEG5000 | 17 (%(w/v)) | |
| 2 | 1 | reservoir | glycerol | 15 (%(v/v)) | |
| 3 | 1 | reservoir | monothioglycerol | 1 (%(v/v)) | |
| 4 | 1 | reservoir | 20 (mM) | ||
| 5 | 1 | reservoir | Tris | 100 (mM) | |
| 6 | 1 | drop | protein | 10 (mg/ml) |
