1X10
Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192A) from a Hyperthermophile, Pyrococcus furiosus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL40B2 |
Synchrotron site | SPring-8 |
Beamline | BL40B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-12-15 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.440, 103.961, 187.494 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
Rwork | 0.227 |
R-free | 0.24810 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ioi |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.048 | 0.083 |
Number of reflections | 62100 | |
<I/σ(I)> | 33 | 15.2 |
Completeness [%] | 96.4 | 86 |
Redundancy | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | PEG4000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |