5X86
Crystal structure of TMP bound thymidylate kinase from thermus thermophilus HB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-09-24 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.8265 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.901, 47.435, 152.062 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.010 - 1.190 |
R-factor | 0.14183 |
Rwork | 0.141 |
R-free | 0.16790 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5x7j |
RMSD bond length | 0.014 |
RMSD bond angle | 1.934 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.010 | 1.210 |
High resolution limit [Å] | 1.190 | 1.190 |
Number of reflections | 108625 | |
<I/σ(I)> | 1.8 | |
Completeness [%] | 99.0 | |
Redundancy | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 295 | 0.2M MgCl2.6H2O, 0.1 M Tris hydrochloride, 30% PEG 4000 |