2PUL
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 | 2004-04-27 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 214.150, 83.470, 51.260 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 65.800 - 2.000 |
| R-factor | 0.20527 |
| Rwork | 0.203 |
| R-free | 0.24012 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.422 |
| 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 | 2.052 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.072 | 0.339 |
| Number of reflections | 59838 | |
| <I/σ(I)> | 14.3 | 5.3 |
| Completeness [%] | 99.8 | 99.7 |
| Redundancy | 7.6 | 7.24 |
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 |
