1UOO
Prolyl oligopeptidase from porcine brain, S554A mutant with bound peptide ligand GLY-PHE-ARG-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 | 70.200, 98.700, 109.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.000 - 2.350 |
| R-factor | 0.195 |
| Rwork | 0.193 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h2z |
| RMSD bond length | 0.006 * |
| RMSD bond angle | 0.900 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 51.000 | 2.430 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.099 | 0.467 |
| Total number of observations | 117435 * | |
| Number of reflections | 31460 | |
| <I/σ(I)> | 12.6 | 2.2 |
| Completeness [%] | 97.6 * | 98.7 |
| Redundancy | 3.9 | 3.8 |
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) |
