5B5G
Crystal structure of ALiS4-Streptavidin complex
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 | 2015-02-02 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 57.921, 84.423, 46.138 |
| Unit cell angles | 90.00, 98.98, 90.00 |
Refinement procedure
| Resolution | 57.210 - 1.500 |
| R-factor | 0.14731 |
| Rwork | 0.145 |
| R-free | 0.19307 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4y59 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.868 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.210 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.058 | 0.352 |
| Number of reflections | 66421 | |
| <I/σ(I)> | 12.8 | 1.9 |
| Completeness [%] | 94.5 | 87.8 |
| Redundancy | 3.2 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1M Tris-HCl (pH8.0), 30%(w/v) PEG 1000, 2.0% agarose hydrogel |
