4GFS
1.8 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium LT2 with Nickel Bound at Active Site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 295 |
| Detector technology | CCD |
| Collection date | 2012-06-04 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97850 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.679, 74.468, 63.566 |
| Unit cell angles | 90.00, 100.17, 90.00 |
Refinement procedure
| Resolution | 29.400 - 1.800 |
| R-factor | 0.20136 |
| Rwork | 0.199 |
| R-free | 0.24925 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3l2i |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.763 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.078 | 0.567 |
| Number of reflections | 40064 | |
| <I/σ(I)> | 13.5 | 1.8 |
| Completeness [%] | 97.1 | 86.8 |
| Redundancy | 3.7 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | Protein solution: 7.5 mg/m, 0.50 sodium phthalate, 0.01 M Tris-HCl (pH 8.3) Screen solution: PEGs II B8 (Qiagen), 0.1 Nickel chloride, 0.1 M Tris pH 8.5, 20% (w/v) PEG 2000 MME , VAPOR DIFFUSION, SITTING DROP, temperature 295K |
