3TOZ
2.2 Angstrom Crystal Structure of Shikimate 5-dehydrogenase from Listeria monocytogenes in Complex with NAD.
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 | 2011-07-14 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 70.130, 78.434, 214.829 |
| Unit cell angles | 90.00, 90.49, 90.00 |
Refinement procedure
| Resolution | 29.630 - 2.200 |
| R-factor | 0.19855 |
| Rwork | 0.195 |
| R-free | 0.25584 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1npd |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.568 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.096 | 0.525 |
| Number of reflections | 117864 | |
| <I/σ(I)> | 12.3 | 2.5 |
| Completeness [%] | 98.2 | 97.3 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | Protein: 7.5mG/mL, 0.25M Sodium chloride, 0.01M TRIS-HCl (pH 8.3); Screen: Classics II (F8), 0.2M Ammonium sulfate, 0.1M HEPES (pH 7.5), 25% (w/v) PEG R3350., VAPOR DIFFUSION, SITTING DROP, temperature 295K |
