6DUB
Crystal structure of a methyltransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-01-23 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 43 |
| Unit cell lengths | 44.359, 44.359, 262.058 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.100 - 1.200 |
| R-factor | 0.1548 |
| Rwork | 0.154 |
| R-free | 0.17780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5e1d |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.823 |
| Data reduction software | HKL-3000 |
| Data scaling software | Aimless (0.5.21) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0218) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 31.140 | 31.140 | 1.220 |
| High resolution limit [Å] | 1.200 | 6.570 | 1.200 |
| Rmerge | 0.074 | 0.062 | 0.973 |
| Rmeas | 0.081 | 0.067 | 1.056 |
| Rpim | 0.032 | 0.026 | 0.404 |
| Total number of observations | 914436 | 6733 | 47423 |
| Number of reflections | 150535 | ||
| <I/σ(I)> | 11 | 32.1 | 2 |
| Completeness [%] | 96.0 | 99 | 93.2 |
| Redundancy | 6.1 | 6.9 | 6.6 |
| CC(1/2) | 0.998 | 0.995 | 0.675 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 30% PEG2000, 0.1 M potassium thiocyanate |
