3ZZG
Crystal structure of the amino acid kinase domain from Saccharomyces cerevisiae acetylglutamate kinase without ligands
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-03 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 68.086, 100.531, 188.740 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.950 |
| R-factor | 0.21357 |
| Rwork | 0.212 |
| R-free | 0.24521 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zzf |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.078 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.110 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.070 | 0.370 |
| Number of reflections | 28023 | |
| <I/σ(I)> | 8.3 | 2.1 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 6.4 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | PROTEIN WAS CRYSTALLIZED IN 50 MM NA-ACETATE, PH 4.6, 0.2 M NA-MALONATE AND 2% PEG 8000,, CONTAINING 24MM N-ACETYLGLUTAMATE (NAG); PREVIOUS TO FREEZING, CRYSTAL WAS WASHED 6 HOURS IN CRYSTALLIZATION BUFFER WITHOUT NAG. 25% GLYCEROL WAS USED AS CRYOPROTECTOR |
