5XAK
Crystal structure (form II) of 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 | 2013-09-25 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9737 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.160, 47.090, 150.940 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.160 - 1.500 |
R-factor | 0.14529 |
Rwork | 0.143 |
R-free | 0.18870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pbr |
RMSD bond length | 0.015 |
RMSD bond angle | 1.728 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.160 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.097 | |
Number of reflections | 53700 | |
<I/σ(I)> | 10.6 | |
Completeness [%] | 99.9 | |
Redundancy | 7.6 | |
CC(1/2) | 0.998 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 295 | CsCl2.H2O, 30% PEG 3500 |