3LT8
A non-biological ATP binding protein with a single point mutation (D65V), that contributes to optimized folding and ligand binding, crystallized in the presence of 100 mM ATP.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12B |
Synchrotron site | NSLS |
Beamline | X12B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-06-18 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 71.461, 71.461, 55.583 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.340 - 2.550 |
R-factor | 0.181 |
Rwork | 0.178 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3G4B |
RMSD bond length | 0.014 |
RMSD bond angle | 1.710 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.640 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.092 | 0.494 |
Number of reflections | 5562 | |
<I/σ(I)> | 25.481 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.6 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 0.1 M SODIUM PHOSPHATE PH 8.5, 0.25 M SODIUM CITRATE, 0.3 M SODIUM CHLORIDE, 23% PEG 400, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K |