1O26
Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and dUMP at 1.6 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL11-1 |
Synchrotron site | SSRL |
Beamline | BL11-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-05-30 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 55.561, 117.730, 141.878 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.600 |
Rwork | 0.203 |
R-free | 0.21800 * |
Structure solution method | MR |
Starting model (for MR) | 1kq4 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.360 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 * | 1.640 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.071 * | 0.539 * |
Total number of observations | 530608 * | |
Number of reflections | 121887 | |
<I/σ(I)> | 15.3 | 1.7 |
Completeness [%] | 98.9 | 91.5 |
Redundancy | 4.3 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 * | 295 | Kuhn, P., (2002) Proteins, 49, 142. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.0 |
2 | 1 | reservoir | PEG200 | 49 (%(w/v)) | or 100mM HEPES, pH7.5 |
3 | 1 | reservoir | PEG200 | 44 (%) |