3OI7
Structure of the structure of the H13A mutant of Ykr043C in complex with sedoheptulose-1,7-bisphosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-22 |
| Detector | RIGAKU SATURN A200 |
| Wavelength(s) | 1.54178 |
| Spacegroup name | P 1 |
| Unit cell lengths | 58.559, 74.945, 83.615 |
| Unit cell angles | 90.04, 89.92, 77.22 |
Refinement procedure
| Resolution | 27.500 - 2.400 |
| R-factor | 0.23007 |
| Rwork | 0.228 |
| R-free | 0.25996 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB 3F3K molecule A protein atoms |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.355 |
| 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] | 50.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.080 | 0.112 |
| Number of reflections | 57671 | |
| <I/σ(I)> | 9.88 | 3.02 |
| Completeness [%] | 82.6 | 36.9 |
| Redundancy | 1.6 | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 294 | 0.1M Hepes 7.5, 10%Iso-propnal, 22%PEG4K, 4%Glycerol, 0.03 mg/ml trypsin, soaking 10min in well solution w/10mM sedoheptulose. Cryoprotected in Paratone-N oil, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
