3LL4
Structure of the H13A mutant of Ykr043C in complex with fructose-1,6-bisphosphate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-12-14 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54178 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 83.620, 84.022, 101.568 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 31.390 - 2.490 |
R-factor | 0.22468 |
Rwork | 0.223 |
R-free | 0.26630 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3F3K molecule A |
RMSD bond length | 0.015 |
RMSD bond angle | 1.554 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.390 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.104 | 0.484 |
Number of reflections | 25181 | |
<I/σ(I)> | 21.28 | 4.7 |
Completeness [%] | 98.0 | 89.1 |
Redundancy | 5 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 294 | resevoir of 0.1M Sodium Hepes ph7.5, 10% isopropanol and 20% PEG4K. 0.03 mg/ml trypsin was added to the protein prior to crystallization setup. Crystals were washed in well solution, then soaked in well solution plus 12% Glycerol and 0.1M fructose 1,6 bis-phosphate at room temperature for 10 minutes prior to flash-freezing in liquid N2, VAPOR DIFFUSION, HANGING DROP, temperature 294K |