3IX6
Crystal structure of Thymidylate synthase thyA from Brucella melitensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-08-17 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 154.600, 62.190, 85.960 |
Unit cell angles | 90.00, 108.88, 90.00 |
Refinement procedure
Resolution | ? - 2.200 |
R-factor | 0.215 |
Rwork | 0.213 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.256 |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 2.260 | |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.051 | 0.362 |
Number of reflections | 39043 | |
<I/σ(I)> | 19.93 | 3.48 |
Completeness [%] | 98.8 | 91.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | JCSG+ condition G6, 0.2 M sodium malonate pH 7.0, 20% PEG 3350, Crystal tracking ID 204287g6, 24.5 mg/mL protein concentration, crystallized with the His6-Smt3 fusion tag still on, VAPOR DIFFUSION, SITTING DROP, temperature 289K |