4FOO
Crystal Structure of Shikimate Dehydrogenase (aroE) Q237K Mutant from Helicobacter pylori
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13C1 |
| Synchrotron site | NSRRC |
| Beamline | BL13C1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2012-05-06 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.808, 46.088, 119.078 |
| Unit cell angles | 90.00, 99.59, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.550 |
| R-factor | 0.1942 |
| Rwork | 0.192 |
| R-free | 0.23100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3phh |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.403 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.640 |
| High resolution limit [Å] | 2.550 | 5.480 | 2.550 |
| Rmerge | 0.085 | 0.048 | 0.312 |
| Number of reflections | 16286 | ||
| <I/σ(I)> | 10.1 | 27.8 | 4.9 |
| Completeness [%] | 99.8 | 99.5 | 99.9 |
| Redundancy | 3.9 | 3.9 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.2M potassium acetate, 0.1M Tris, 23% PEG 3350 , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
