1E98
Wild type human thymidylate kinase complexed with AZTMP and ADP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Temperature [K] | 100 |
Detector technology | AREA DETECTOR |
Detector | SIEMENS MULTIWIRE |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 101.050, 101.050, 49.950 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.900 |
R-factor | 0.191 * |
Rwork | 0.191 |
R-free | 0.24200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.800 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.080 * | 0.276 * |
Total number of observations | 57280 * | |
Number of reflections | 20180 | |
<I/σ(I)> | 11.8 | 2.1 |
Completeness [%] | 96.3 | 94.2 |
Redundancy | 2.84 | 1.93 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | 20 * | Ostermann, N., (2000) Structure (London), 8, 629. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | nucleotide | ||
2 | 1 | drop | TMPK | 28 (mg/ml) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | drop | 200 (mM) | ||
5 | 1 | drop | Tris-HCl | 50 (mM) | |
6 | 1 | reservoir | PEG3350 | 15-22 (%(w/v)) | |
7 | 1 | reservoir | dead sea water | 5 (%(v/v)) | |
8 | 1 | reservoir | Tris-HCl | 100 (mM) |