1V4A
Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-02-05 |
Wavelength(s) | 0.95372, 0.97844, 0.97855 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 116.836, 116.836, 67.744 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.22993 |
Rwork | 0.228 |
R-free | 0.26900 |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.076 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.083 | 0.517 |
Number of reflections | 36424 | |
<I/σ(I)> | 8.9 | 5.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 35 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 294 | PEG 2000 MME, sodium formate, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |