1X12
Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192D) 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 | 47.451, 103.845, 187.056 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
Rwork | 0.214 |
R-free | 0.23900 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 1x10 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
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 | 0.027 | 0.044 |
Number of reflections | 62491 | |
<I/σ(I)> | 38.7 | 23.7 |
Completeness [%] | 97.9 | 96.9 |
Redundancy | 4.9 |
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 |