1WX0
Crystal structure of transaldolase from Thermus thermophilus HB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-10-22 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 93.693, 142.702, 96.595 |
Unit cell angles | 90.00, 114.46, 90.00 |
Refinement procedure
Resolution | 29.600 - 2.270 |
R-factor | 0.198 |
Rwork | 0.196 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1L6W.pdb |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.350 |
High resolution limit [Å] | 2.270 | 2.270 |
Rmerge | 0.108 | 0.548 |
Number of reflections | 105189 | |
<I/σ(I)> | 9.5 | 3.59 |
Completeness [%] | 99.2 | 98.4 |
Redundancy | 3.9 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 8.5 | 291 | Magnesium Chloride, Tris Hydrochloride, PEG 4000, Glycerol, pH 8.5, MICROBATCH, temperature 291K |