1TXJ
Crystal structure of translationally controlled tumour-associated protein (TCTP) from Plasmodium knowlesi
Experimental procedure
Experimental method | MAD |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-04-25 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 65 |
Unit cell lengths | 86.633, 86.633, 55.636 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.860 - 2.000 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.23400 |
Structure solution method | MAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.500 |
Data reduction software | d*TREK |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.043 | 0.314 |
Number of reflections | 16150 | |
<I/σ(I)> | 54.1 | 8.3 |
Completeness [%] | 99.7 | 100 |
Redundancy | 7.7 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | sodium citrate, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |