7JHK
Structure of human beta 1,3-N-acetylglucosaminyltransferase 2 in unliganded form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 87 |
Detector technology | CCD |
Collection date | 2017-12-13 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 67.416, 80.070, 157.614 |
Unit cell angles | 90.00, 98.82, 90.00 |
Refinement procedure
Resolution | 47.185 - 2.344 |
R-factor | 0.1811 |
Rwork | 0.179 |
R-free | 0.21730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7jhi |
RMSD bond length | 0.004 |
RMSD bond angle | 0.660 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 100.000 | 100.000 | 2.390 |
High resolution limit [Å] | 2.344 | 6.380 | 2.350 |
Rmerge | 0.070 | 0.036 | 0.437 |
Rmeas | 0.078 | 0.041 | 0.508 |
Rpim | 0.035 | 0.018 | 0.256 |
Number of reflections | 66967 | 3616 | 2565 |
<I/σ(I)> | 7.4 | ||
Completeness [%] | 95.7 | 99.2 | 74.2 |
Redundancy | 4.6 | 4.9 | 3.6 |
CC(1/2) | 0.998 | 0.899 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277 | 24% PEG1500, 20% glycerol |