3ZZF
Crystal structure of the amino acid kinase domain from Saccharomyces cerevisiae acetylglutamate kinase complexed with its substrate N- acetylglutamate
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 | 2009-07-25 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.701, 99.299, 190.644 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.1807 |
| Rwork | 0.179 |
| R-free | 0.21812 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | STARTING MODEL WAS A LOW RESOLUTION INCOMPLETE MODEL FROM A SE-MET SUBSTITUTED CRYSTAL |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.038 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.970 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.120 | 0.400 |
| Number of reflections | 67865 | |
| <I/σ(I)> | 5 | 1.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 15 | 15.3 |
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; PREVIOUS TO FREEZING, CRYSTAL WAS SOAKED IN 2 MM HGCL2 AND 25% GLYCEROL AS CRYOPROTECTOR |
