1O28
Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FdUMP at 2.1 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-04-14 |
Detector | ADSC QUANTUM 4r |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.390, 116.709, 141.003 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.100 |
Rwork | 0.193 |
R-free | 0.24000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1kq4 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.220 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.600 * | 2.150 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.065 * | 0.445 * |
Total number of observations | 161945 * | |
Number of reflections | 50458 | |
<I/σ(I)> | 12.1 | 2.3 |
Completeness [%] | 95.2 | 86.3 |
Redundancy | 3.2 | 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 (%) |