5LFU
Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full extracellular domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2) |
Synchrotron site | PETRA III, EMBL c/o DESY |
Beamline | P14 (MX2) |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-12-15 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.97553 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 101.237, 101.237, 687.477 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 114.579 - 4.300 |
R-factor | 0.2859 |
Rwork | 0.285 |
R-free | 0.29550 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1url 4frw 1cs6 3p3y 2yd6 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.331 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 114.620 | 4.810 |
High resolution limit [Å] | 4.300 | 4.300 |
Rmerge | 0.115 | 3.937 |
Number of reflections | 15430 | |
<I/σ(I)> | 15.6 | 1.3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 35.7 | 36.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | Crystals were grown from protein that was modified by reductive lysine methylation. Protein was concentrated to 8.4 mg/mL, which was mixed 1:1 with reservoir solution. Crystals grew in a condition containing 200 mM NaOAc and 20 % PEG3350 (w/v). |