5B5F
Crystal structure of ALiS3-Streptavidin complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-01-20 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.9 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 57.985, 84.621, 46.336 |
Unit cell angles | 90.00, 99.00, 90.00 |
Refinement procedure
Resolution | 57.270 - 1.200 |
R-factor | 0.155 |
Rwork | 0.153 |
R-free | 0.19300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4y59 |
RMSD bond length | 0.021 |
RMSD bond angle | 2.061 |
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] | 57.270 | 1.220 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.048 | 0.482 |
Number of reflections | 134521 | |
<I/σ(I)> | 13.2 | 1.8 |
Completeness [%] | 98.0 | 96.3 |
Redundancy | 4 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1M MES-NaOH (pH6.0), 35%(w/v) PEG 1000, 2.0% agarose hydrogel |