3AHP
Crystal structure of stable protein, CutA1, from a psychrotrophic bacterium Shewanella sp. SIB1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-13 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 134.671, 134.671, 128.410 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.700 |
| R-factor | 0.20798 |
| Rwork | 0.205 |
| R-free | 0.26059 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1naq |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.312 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.750 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.175 | 0.772 |
| Number of reflections | 33076 | |
| <I/σ(I)> | 18.8 | 3.03 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 14.6 | 14.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 2.0M Na/K-phosphate, 100mM acetate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
