3BHD
Crystal structure of human thiamine triphosphatase (THTPA)
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-09-13 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97915 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 60.770, 46.810, 71.870 |
Unit cell angles | 90.00, 113.97, 90.00 |
Refinement procedure
Resolution | 19.960 - 1.500 |
R-factor | 0.17774 |
Rwork | 0.176 |
R-free | 0.20117 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.605 |
Data scaling software | XSCALE |
Phasing software | SHELX |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.600 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.061 | 0.421 |
Number of reflections | 115663 | |
<I/σ(I)> | 13.79 | 3.1 |
Completeness [%] | 99.6 | 99.7 |
Redundancy | 3.51 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 3.8 | 300 | 50mM Citric acid, 0.2M Ammonium sulfate, 3mM Sodium tungstenate, 10mg/ml Protein, pH 3.8, VAPOR DIFFUSION, SITTING DROP, temperature 300K |