4QPN
Crystal Structure of Human Methyltransferase-Like Protein 21B
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-06-12 |
Detector | adsc q315 |
Wavelength(s) | 0.97915 |
Spacegroup name | P 61 |
Unit cell lengths | 38.665, 38.665, 193.915 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 33.480 - 1.250 |
R-factor | 0.1238 |
Rwork | 0.122 |
R-free | 0.16670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | solved with data from isomorphous crystal. model based on pdb entry 4LEC. |
RMSD bond length | 0.019 |
RMSD bond angle | 1.980 |
Data reduction software | XDS |
Data scaling software | Aimless (0.3.5) |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.780 | 1.270 |
High resolution limit [Å] | 1.250 | 1.250 |
Rmerge | 0.092 | 0.956 |
Total number of observations | 23595 | |
Number of reflections | 45170 | |
<I/σ(I)> | 19.6 | 3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.1 | 10.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 293 | 20% PEG-3350, 0.2 M tri-lithium citrate. Protein sample was incubated with SAH overnight. Endopeptidase was added to the protein sample immediately prior to crystallization set up, vapor diffusion, temperature 293K |