2PUP
Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-02-15 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 213.930, 83.290, 51.420 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.340 - 2.600 |
| R-factor | 0.21387 |
| Rwork | 0.211 |
| R-free | 0.27410 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.591 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 107.210 | 2.667 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.098 | 0.358 |
| Number of reflections | 27245 | |
| <I/σ(I)> | 9.8 | 3.4 |
| Completeness [%] | 98.3 | 99.6 |
| Redundancy | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 22% PEG 2000MME, 0.3M sodium acetate, 0.1M TrisHCl, 8mM CHAPS, 10mM ATP, 2mM magnesium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
