3TKF
1.5 Angstrom Resolution Crystal Structure of K135M Mutant of Transaldolase B (TalA) from Francisella tularensis in Complex with Sedoheptulose 7-phosphate.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-08-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.827, 87.194, 141.136 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.670 - 1.500 |
| R-factor | 0.14459 |
| Rwork | 0.144 |
| R-free | 0.15866 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3te9 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.517 |
| 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 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.069 | 0.452 |
| Number of reflections | 109948 | |
| <I/σ(I)> | 23.1 | 3.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.2 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | Protein:9.4mG/mL, 0.5M Sodium chloride, 0.1M TRIS-HCl (pH 8.3), 0.015M Sedoheptulose 7-phosphate; Screen: PEG's (B6), 0.1M HEPES, 25% (w/v) PEG2000 MME., VAPOR DIFFUSION, SITTING DROP, temperature 295K |
