1NMX
Crystal structure of human thymidylate kinase with FLTMP and ADP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Wavelength(s) | 0.9076 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 101.515, 101.515, 50.012 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.100 - 1.700 |
Rwork | 0.183 |
R-free | 0.22800 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.013 * |
RMSD bond angle | 1.400 * |
Data reduction software | XDS |
Data scaling software | XDS |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 32.100 | 1.800 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.080 | 0.283 * |
Total number of observations | 137414 * | |
Number of reflections | 28602 | |
<I/σ(I)> | 10.6 | 3.94 |
Completeness [%] | 97.5 | 99.3 |
Redundancy | 4.8 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | PEG 3350, 100 mM Tris/HCl pH 8.0, 5% sterile filtered dead sea water, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2 (mM) | |
2 | 1 | drop | ADP | 2 (mM) |