2CBG
Crystal structure of the PMSF-inhibited thioesterase domain of the fengycin biosynthesis cluster
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR591 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-10-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 |
| Unit cell lengths | 72.354, 72.354, 96.333 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 24.000 - 2.500 |
| R-factor | 0.166 |
| Rwork | 0.162 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jmk |
| RMSD bond length | 0.041 |
| RMSD bond angle | 2.589 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.000 | 2.560 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.080 | 0.220 |
| Number of reflections | 9190 | |
| <I/σ(I)> | 20.2 | 4.4 |
| Completeness [%] | 91.6 | 54.9 |
| Redundancy | 3.76 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.6 | 0.2 M NH4 ACETATE, 0.1 M NA CITRATE (PH 5.6), 22.5 % PEG 8000, 10 MG/ML PROTEIN |
