4LG1
Human Methyltransferase-Like Protein 21D
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 | 2013-06-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.783, 100.052, 96.193 |
| Unit cell angles | 90.00, 101.25, 90.00 |
Refinement procedure
| Resolution | 33.750 - 1.800 |
| R-factor | 0.1963 |
| Rwork | 0.196 |
| R-free | 0.22210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bzb |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.321 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.070 | 0.034 | 0.787 |
| Number of reflections | 75014 | ||
| <I/σ(I)> | 11.3 | ||
| Completeness [%] | 91.3 | 96.8 | 88.7 |
| Redundancy | 5.3 | 5.3 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 23% PEG 3350, 0.2 M Lithium Sulfate, 0.1 M BisTris pH6.5, vapor diffusion hanging drop, temperature 291K |
