5L0Y
Crystal Structure of a Sec72-ssa1 c-terminal peptide fusion protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-07-16 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 1.0332 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 76.504, 118.535, 164.049 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 96.080 - 2.870 |
R-factor | 0.238 |
Rwork | 0.236 |
R-free | 0.28300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5l0w |
RMSD bond length | 0.007 |
RMSD bond angle | 1.060 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 164.050 |
High resolution limit [Å] | 2.870 |
Number of reflections | 34691 |
<I/σ(I)> | 16 |
Completeness [%] | 99.3 |
Redundancy | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 295 | 0.1 M ammonium citrate pH 7.0, 12% PEG 3350 |