6LNG
Rapid crystallization of streptavidin using charged peptides
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 | 2014-11-22 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 81.293, 80.829, 132.648 |
Unit cell angles | 90.00, 99.85, 90.00 |
Refinement procedure
Resolution | 37.088 - 1.800 |
R-factor | 0.183059438376 |
Rwork | 0.181 |
R-free | 0.21863 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ry1 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.124 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.100 | 1.850 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.064 | 0.390 |
Number of reflections | 78148 | 5742 |
<I/σ(I)> | 13.91 | 3.1 |
Completeness [%] | 99.7 | |
Redundancy | 3.67 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | BATCH MODE | 298 | 0.2 M ammonium sulfate, 0.1 M MES pH 6.5, 30% w/v polyethylene glycol monomethyl ether 5000 |