3VAA
1.7 Angstrom Resolution Crystal Structure of Shikimate Kinase from Bacteroides thetaiotaomicron
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 | 2011-12-09 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.253, 46.460, 105.124 |
| Unit cell angles | 90.00, 97.42, 90.00 |
Refinement procedure
| Resolution | 29.060 - 1.700 |
| R-factor | 0.16527 |
| Rwork | 0.163 |
| R-free | 0.19923 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pt5 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.287 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.059 | 0.495 |
| Number of reflections | 64576 | |
| <I/σ(I)> | 17.8 | 2.09 |
| Completeness [%] | 99.5 | 93.8 |
| Redundancy | 3.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | Protein: 7.5 mg/mL, 0.25M Sodium chloride, Tris-HCl pH 8.3, Screen: Classics II (C9), 1.1M Sodium malonate, 0.1M HEPES pH 7.0, 0.5% (v/v) Jeffamine ED-2001, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
