3LD9
Crystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-02 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9744 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 39.170, 144.820, 146.840 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.370 - 2.150 |
R-factor | 0.18883 |
Rwork | 0.187 |
R-free | 0.23220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2PBR MODIFIED WITH CCP4 PROGRAM CHAINSAW |
RMSD bond length | 0.014 |
RMSD bond angle | 1.345 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.210 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.079 | 0.481 |
Number of reflections | 46708 | |
<I/σ(I)> | 16.84 | 3.7 |
Completeness [%] | 100.0 | 99.9 |
Redundancy | 5.9 | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 290 | MD PACT SCREEN G8: 100MM BIS-TRIS-PROPANE PH 7.5, 200MM NA-SULPHATE, 20% PEG 3350; EHCHA.01616.A AT 25.5MG/ML, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K |