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). |