2BKL
Structural and Mechanistic Analysis of Two Prolyl Endopeptidases: Role of Inter-Domain Dynamics in Catalysis and Specificity
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-12-19 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.692, 114.718, 99.279 |
| Unit cell angles | 90.00, 103.60, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.500 |
| R-factor | 0.161 |
| Rwork | 0.160 |
| R-free | 0.18200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qfs |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.491 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.070 | 0.470 |
| Number of reflections | 225366 | |
| <I/σ(I)> | 12.8 | 2.8 |
| Completeness [%] | 98.9 | 97.7 |
| Redundancy | 4.1 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 26% METHOXY PEG 5K AND 0.1MES (PH 6.01). |
