2PUI
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 | 2005-06-17 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 213.780, 83.530, 51.240 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 65.820 - 2.200 |
R-factor | 0.2012 |
Rwork | 0.199 |
R-free | 0.24883 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.012 |
RMSD bond angle | 1.404 |
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] | 106.600 | 2.257 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.080 | 0.302 |
Number of reflections | 44738 | |
<I/σ(I)> | 17.3 | 8 |
Completeness [%] | 98.9 | 95.5 |
Redundancy | 13.7 | 12.74 |
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 |