Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-10-01 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 219.990, 45.946, 90.105 |
Unit cell angles | 90.00, 111.46, 90.00 |
Refinement procedure
Resolution | 102.370 - 3.230 |
R-factor | 0.219 |
Rwork | 0.217 |
R-free | 0.25300 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.120 |
Data reduction software | Aimless |
Data scaling software | SCALA |
Phasing software | REFMAC |
Refinement software | BUSTER (2.11.7) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 102.370 | 102.370 |
High resolution limit [Å] | 3.230 | 3.230 |
Number of reflections | 13837 | |
<I/σ(I)> | 8.2 | |
Completeness [%] | 99.5 | |
Redundancy | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | PROTEIN WAS CONCENTRATED TO 6 MG/ML, AND THEN MIXED AT A 2:1 RATIO WITH PEG 3350 (18-20% V/V), 0.2 M AMMONIUM CITRATE (PH 7) IN A SITTING DROP WELL AT 277 K. CRYOPROTECTANT WAS MADE USING MOTHER LIQUOR AT A FINAL CONCENTRATION OF 23% PEG 3350., VAPOR DIFFUSION, SITTING DROP |