2EBJ
Crystal structure of pyrrolidone carboxyl peptidase from Thermus thermophilus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 180 |
Detector technology | CCD |
Collection date | 2006-07-07 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 51.913, 118.382, 143.581 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.820 - 1.900 |
R-factor | 0.228 |
Rwork | 0.228 |
R-free | 0.25700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1iof |
RMSD bond length | 0.005 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.037 | 0.061 |
Number of reflections | 34291 | |
Completeness [%] | 97.6 | 97.9 |
Redundancy | 6.4 | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 0.1M Bis-tris Propane 7.0, 1.2M DL Malic Acid, VAPOR DIFFUSION, SITTING DROP, temperature 293K |