6L1N
Substrate bound BacF structure from Bacillus subtillis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-09-29 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9840 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 71.290, 56.910, 78.500 |
Unit cell angles | 90.00, 97.86, 90.00 |
Refinement procedure
Resolution | 77.760 - 2.000 |
R-factor | 0.1844 |
Rwork | 0.182 |
R-free | 0.23940 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2o1b |
RMSD bond length | 0.016 |
RMSD bond angle | 1.585 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 77.760 | 2.072 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 42411 | 4243 |
<I/σ(I)> | 15.46 | |
Completeness [%] | 100.0 | |
Redundancy | 6.3 | |
CC(1/2) | 0.991 | 0.737 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 295 | 0.1M sodium acetate trihydrate, 0.1M cacodylate trihydrate (pH= 6.5), 30% w/v polyethylene glycol |