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 |