2WEW
Crystal structure of human apoM in complex with myristic acid
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | RAYONICS |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 49.940, 49.940, 144.670 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.950 |
R-factor | 0.21112 |
Rwork | 0.208 |
R-free | 0.26746 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.015 |
RMSD bond angle | 1.610 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHELXCDE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.060 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.050 | 0.360 |
Number of reflections | 13952 | |
<I/σ(I)> | 25.18 | 4.84 |
Completeness [%] | 98.4 | 91.3 |
Redundancy | 7.06 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.2 | ABOUT 1-2 MICROL OF PROTEIN (10-16 MG/ML IN 20 MM TRIS-HCL, PH 7.2) WERE MIXED WITH 1-2 MICROL OF 30 % PEG1500 (W/V, IN DEIONISED WATER) AND EQUILIBRATED AGAINST 700 MICROL OF RESERVOIR SOLUTION CONTAINING 30 % PEG1500. |