2OLS
The crystal structure of the phosphoenolpyruvate synthase from Neisseria meningitidis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-20 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97980 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 183.046, 183.046, 72.245 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.220 - 2.400 |
R-factor | 0.20058 |
Rwork | 0.198 |
R-free | 0.25087 |
Structure solution method | SAD |
RMSD bond length | 0.016 |
RMSD bond angle | 1.705 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 129.100 | 2.462 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.112 | 0.700 |
Number of reflections | 40537 | |
<I/σ(I)> | 21.46 | 1.6 |
Completeness [%] | 88.1 | 56.33 |
Redundancy | 15.8 | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.2M Potassium nitrate, 2.2M Ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 298K |