4FOS
Crystal Structure of Shikimate Dehydrogenase (aroE) Q237A Mutant from Helicobacter pylori in Complex with Shikimate
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 | 2012-04-21 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.311, 62.718, 84.030 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.720 |
| R-factor | 0.1731 |
| Rwork | 0.172 |
| R-free | 0.19890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3phg |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.467 |
| Data reduction software | DENZO |
| 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 | 1.780 |
| High resolution limit [Å] | 1.720 | 3.700 | 1.720 |
| Rmerge | 0.046 | 0.028 | 0.297 |
| Number of reflections | 26472 | ||
| <I/σ(I)> | 16.8 | 56 | 6.5 |
| Completeness [%] | 99.3 | 99.4 | 97.4 |
| Redundancy | 6.7 | 6.8 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.2M sodium acetate, 0.1M Tris, 36% PEG 4000 , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
