1R4V
1.9A crystal structure of protein AQ328 from Aquifex aeolicus
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 | 2003-08-23 |
| Detector | SBC-2 |
| Wavelength(s) | 0.95372, 0.97932, 0.97952 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 56.036, 56.036, 244.768 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.1822 |
| Rwork | 0.181 |
| R-free | 0.21311 |
| Structure solution method | MAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.722 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.9999) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.098 | 0.570 |
| Number of reflections | 17815 | |
| Completeness [%] | 93.1 | 50.9 |
| Redundancy | 11.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | PEG 3350, sodium chloride, Zinc Acetate, cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
