2RD5
Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-24 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.3361 |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 171.133, 171.133, 171.133 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.510 |
| R-factor | 0.20261 |
| Rwork | 0.201 |
| R-free | 0.22928 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb entries 2BUF 2o66 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.291 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.127 | 0.950 |
| Number of reflections | 57349 | |
| <I/σ(I)> | 38 | 3.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 17.7 | 14.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 8.5% PEG 8000, 8.5% PEG 1000, 0.1 M Na-HEPES, 0.4 M TMAO, 50 mM L-aginine, 2 mM DTT, 12% (w/v) glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
