5O1M
Structure of Latex Clearing Protein LCP in the closed state
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-06-13 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 1.73672 |
Spacegroup name | P 1 |
Unit cell lengths | 54.863, 56.544, 63.861 |
Unit cell angles | 74.25, 86.07, 71.04 |
Refinement procedure
Resolution | 61.450 - 2.200 |
R-factor | 0.1769 |
Rwork | 0.174 |
R-free | 0.22270 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.020 |
RMSD bond angle | 2.007 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 61.450 | 2.270 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.065 | |
Rpim | 0.039 | 0.180 |
Number of reflections | 30914 | |
<I/σ(I)> | 12.3 | 3.8 |
Completeness [%] | 87.2 | 83.7 |
Redundancy | 3.7 | 3.7 |
CC(1/2) | 0.997 | 0.932 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298.15 | 16 % (w/v) PEG 3350, 0.2 M L-proline, 0.1 M HEPES/NaOH |