1TQP
Crystal Structure of A. fulgidus Rio2 Serine Protein Kinase Bound to ATP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-01-16 |
Detector | MARRESEARCH |
Wavelength(s) | 1.54 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 116.141, 44.512, 62.687 |
Unit cell angles | 90.00, 93.95, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.100 |
R-factor | 0.16756 |
Rwork | 0.165 |
R-free | 0.21520 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tqi |
RMSD bond length | 0.032 |
RMSD bond angle | 2.451 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.700 | 2.155 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 18666 | |
<I/σ(I)> | 26.78 | 9.17 |
Completeness [%] | 98.6 | 97.8 |
Redundancy | 4.1 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 3.83 | 293 | PEG 900, SODIUM PHOSPHATE, SODIUM CITRATE, pH 3.83, VAPOR DIFFUSION, HANGING DROP, temperature 293K |