1O25
Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with dUMP at 2.4 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 | 2002-04-15 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.682, 116.703, 141.727 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.400 |
| Rwork | 0.199 |
| R-free | 0.26300 * |
| Structure solution method | MR |
| 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] | 54.400 * | 2.460 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.091 * | 0.338 * |
| Total number of observations | 134682 * | |
| Number of reflections | 33587 | |
| <I/σ(I)> | 14.1 | 2.9 |
| Completeness [%] | 93.0 | 85.6 |
| Redundancy | 4 | 3.4 |
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 (%) |
