2R8V
Native structure of N-acetylglutamate synthase from Neisseria gonorrhoeae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Detector technology | CCD |
Collection date | 2007-06-18 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.000 |
Spacegroup name | P 3 1 2 |
Unit cell lengths | 98.661, 98.661, 89.755 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.19438 |
Rwork | 0.192 |
R-free | 0.25234 |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 2.041 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXS |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.097 | 0.584 |
Number of reflections | 17297 | |
<I/σ(I)> | 30.6 | 2 |
Completeness [%] | 99.1 | 98.8 |
Redundancy | 10.9 | 8.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.8 | 291 | 25% PEG3350, 100mM CsCl, 100 MM sodium citrate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K |