2PUN
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 | 2004-11-09 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 214.730, 83.620, 51.170 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.170 - 2.300 |
| R-factor | 0.20423 |
| Rwork | 0.202 |
| R-free | 0.25456 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.468 |
| 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] | 105.410 | 2.360 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.069 | 0.263 |
| Number of reflections | 39577 | |
| <I/σ(I)> | 15.4 | 6.6 |
| Completeness [%] | 99.3 | 98.4 |
| Redundancy | 7.5 |
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, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
