7FGQ
Crystal structure of Thymidylate kinase with TMP and its low-resolution (SAXS) solution structure from Brugia malayi
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 11.2C |
Synchrotron site | ELETTRA |
Beamline | 11.2C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-03-15 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97840 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 58.670, 58.670, 119.610 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.881 - 1.910 |
R-factor | 0.221 |
Rwork | 0.220 |
R-free | 0.24860 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e9c |
RMSD bond length | 0.008 |
RMSD bond angle | 1.080 |
Data reduction software | iMOSFLM (7.0.072) |
Data scaling software | Aimless (7.0.072) |
Phasing software | PHENIX (2.8.2) |
Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.881 | 8.960 |
High resolution limit [Å] | 1.910 | 1.910 |
Rmerge | 0.092 | 1.107 |
Rmeas | 0.101 | |
Rpim | 0.040 | 0.504 |
Number of reflections | 16977 | 16977 |
<I/σ(I)> | 2.2 | 2.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.2 | 10.7 |
CC(1/2) | 0.999 | 0.741 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 300 | Diammonium tartrate, Bis-Tris pH 6.0 |