3PGJ
2.49 Angstrom resolution crystal structure of shikimate 5-dehydrogenase (aroE) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with shikimate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-10-20 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 75.527, 83.657, 79.585 |
| Unit cell angles | 90.00, 93.51, 90.00 |
Refinement procedure
| Resolution | 28.800 - 2.490 |
| R-factor | 0.19609 |
| Rwork | 0.193 |
| R-free | 0.24711 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3o8q |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.416 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.540 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.058 | 0.525 |
| Number of reflections | 34293 | |
| <I/σ(I)> | 20.77 | 2.41 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 295 | Protein: 7.5 mg/mL in 10 mM Tris/HCl pH 8.3, 0.5 M NaCl, 5 mM BME. Crystallization condition: The Classic suite H3 (#87) condition (0.2 M Ammonium acetate, 0.1 M tri-Sodium citrate pH 5.6, 30 % (w/v) PEG4000). Crystal was soaked in 25 mM shikimate. , VAPOR DIFFUSION, SITTING DROP, temperature 295K |
