5AZH
Crystal structure of LGG-2 fused with an EEEWEEL peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL32XU |
Synchrotron site | SPring-8 |
Beamline | BL32XU |
Temperature [K] | 95 |
Detector technology | CCD |
Collection date | 2015-09-28 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 35.532, 55.193, 72.592 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.940 - 2.300 |
R-factor | 0.23826 |
Rwork | 0.236 |
R-free | 0.28827 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.245 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.940 | 2.240 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.104 | 0.859 |
Number of reflections | 7374 | |
<I/σ(I)> | 29.3 | |
Completeness [%] | 98.3 | 85.9 |
Redundancy | 18.4 | 14.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | sodium chloride, magnesium chloride, HEPES |