1E9F
Mutant human thymidylate kinase complexed with TMP and ADP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7B |
Temperature [K] | 100 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 100.200, 100.200, 49.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 70.000 - 1.900 |
R-factor | 0.226 * |
Rwork | 0.226 |
R-free | 0.28300 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond angle | 2.890 * |
Data reduction software | XDS |
Data scaling software | XSCALE |
Refinement software | REFMAC (5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.054 * | 0.144 * |
Total number of observations | 96858 * | |
Number of reflections | 19646 | |
<I/σ(I)> | 17 | 3.2 |
Completeness [%] | 96.8 | 97.3 |
Redundancy | 4.9 | 4.3 |
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) |