3D2M
Crystal structure of N-acetylglutamate synthase from Neisseria gonorrhoeae complexed with coenzyme A and L-glutamate
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 | IMAGE PLATE |
| Collection date | 2008-03-19 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 3 1 2 |
| Unit cell lengths | 98.802, 98.802, 90.107 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.210 |
| R-factor | 0.23108 |
| Rwork | 0.229 |
| R-free | 0.28030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3b8g |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.789 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.170 | 2.290 |
| High resolution limit [Å] | 2.210 | 2.210 |
| Rmerge | 0.070 | 0.734 |
| Number of reflections | 24544 | |
| <I/σ(I)> | 37.5 | 1.3 |
| Completeness [%] | 96.5 | 72.9 |
| Redundancy | 10.1 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6.4 | 291 | 8% PEG3350, 100 mM ammonium citrate, pH 6.4, EVAPORATION, temperature 291K |
