1OHB
Acetylglutamate kinase from Escherichia coli complexed with ADP and sulphate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-11-01 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 59.242, 71.449, 107.230 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.890 - 1.900 |
R-factor | 0.1948 |
Rwork | 0.195 |
R-free | 0.22110 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gs5 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.890 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.075 | 0.357 |
Total number of observations | 100167 * | |
Number of reflections | 18284 | |
<I/σ(I)> | 9.7 | 2.1 |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.5 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 4.6 | 27-29% POLYETHYLENE GLYCOL MONOMETHYL ETHER 2K, SODIUM ACETATE 0.1M PH 4.6 AMMONIUM SULPHATE 0.15-0.3 M |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG2000 | 27-29 (%(w/v)) | |
2 | 1 | reservoir | sodium acetate | 0.1 (M) | pH4.6 |
3 | 1 | reservoir | ammonium citrate | 0.15-0.3 (M) | |
4 | 1 | drop | protein | 10 (mg/ml) |