3ZZI
Crystal structure of a tetrameric acetylglutamate kinase from Saccharomyces cerevisiae
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 1 |
Unit cell lengths | 95.240, 111.290, 113.140 |
Unit cell angles | 75.77, 89.29, 69.12 |
Refinement procedure
Resolution | 109.110 - 3.800 |
R-factor | 0.19914 |
Rwork | 0.197 |
R-free | 0.23592 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ZZF FOR ONE DOMAIN AND AN INCOMPLETE TRACING FROM OTHER CRYSTAL OF THE SAME PRESENT PROTEIN FOR THE SECOND DOMAIN |
RMSD bond length | 0.015 |
RMSD bond angle | 1.793 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 109.000 | 4.010 |
High resolution limit [Å] | 3.800 | 3.800 |
Rmerge | 0.057 | 0.455 |
Number of reflections | 39773 | |
<I/σ(I)> | 10.5 | 1.5 |
Completeness [%] | 96.3 | 96.3 |
Redundancy | 2.4 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 277 | PROTEIN WAS SUBJECTED TO REDUCTIVE METHYLATION OF SURFACE EXPOSED LYSINES WITH ABC PREVIOUS TO CRYSTALLIZATION. 10 MG/ML PROTEIN IN 20MM HEPES PH 7.5, 0.5 M NACL, 1MM MSH, AND SUPPLEMENTED WITH 40 MM NAG, WAS CRYSTALLIZED IN PRESENCE OF 0.2 M AMMONIUM CITRATE PH 7.0 AND 12 % PEG3350 AS CRYSTALLIZATION SOLUTION, IN SITTING DROPS AT 4C. CRYOBUFFER SOLUTION WAS THAT OF CRYSTALLIZATION WITH PEG3350 ENRICHED TO 40 %. |