3TK7
2.0 Angstrom Resolution Crystal Structure of Transaldolase B (TalA) from Francisella tularensis in Covalent Complex with Fructose 6-Phosphate
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 | 2011-08-04 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.123, 74.257, 164.995 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.990 - 2.000 |
| R-factor | 0.18765 |
| Rwork | 0.185 |
| R-free | 0.23205 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3igx |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.188 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.084 | 0.474 |
| Number of reflections | 47501 | |
| <I/σ(I)> | 18.8 | 3.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.9 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 295 | Protein: 11.2 mg/ml, 0.5 M sodium chloride, 0.01 M Tris-HCl (pH 8.3), 0.005 M Fructose 6-phosphate Screen: Classics II D6 (Qiagen), 0.1 M Bis-tris, 25% (w/v) PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K |






