2X2W
Acetylglutamate kinase from Escherichia coli bound to N-acetyl-L-glutamyl-5-phosphate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-07-01 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 78.652, 78.652, 283.054 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.2 |
Rwork | 0.199 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wxb |
RMSD bond length | 0.009 |
RMSD bond angle | 1.168 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 (K) |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.240 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 35550 | |
<I/σ(I)> | 44 | 6.3 |
Completeness [%] | 99.8 | 100 |
Redundancy | 12.6 | 11.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 294 | 30-35 % PEG MONOMETHYL ETHER 5K, 0.1 M MES PH 6.5, 0.1-0.2 M (NH4)2SO4 |