6HP2
Crystal Structure of the O-Methyltransferase from the trans-AT PKS multienzyme C0ZGQ3 of Brevibacillus brevis in complex with S-Adenosyl-L-homocysteine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-07-12 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.99998 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.382, 71.256, 61.396 |
| Unit cell angles | 90.00, 104.90, 90.00 |
Refinement procedure
| Resolution | 45.595 - 1.900 |
| R-factor | 0.1601 |
| Rwork | 0.158 |
| R-free | 0.20240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6hp1 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.137 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.595 | 1.968 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.129 | 1.319 |
| Rmeas | 0.134 | 1.401 |
| Rpim | 0.037 | 0.464 |
| Number of reflections | 29127 | 2819 |
| <I/σ(I)> | 11.5 | 1.5 |
| Completeness [%] | 99.6 | 96.44 |
| Redundancy | 12.7 | 8.7 |
| CC(1/2) | 0.998 | 0.650 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M Na K Phosphate, 0.1M BisTrisPropane, 18.5% PEG3350 |
