4FPX
Crystal Structure of Shikimate Dehydrogenase (aroE) Q237N Mutant from Helicobacter pylori
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2012-06-05 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.614, 46.035, 119.187 |
| Unit cell angles | 90.00, 99.52, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.400 |
| R-factor | 0.1951 |
| Rwork | 0.193 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3phg |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.387 |
| 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 | 2.490 |
| High resolution limit [Å] | 2.400 | 5.160 | 2.400 |
| Rmerge | 0.088 | 0.050 | 0.336 |
| Number of reflections | 18960 | ||
| <I/σ(I)> | 10.6 | 19 | 3.7 |
| Completeness [%] | 97.3 | 95.4 | 95.4 |
| Redundancy | 3.5 | 3.3 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.2M sodium acetate, 0.1M Tris, 36% PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
