2CB9
Crystal structure of the 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 | 2003-09-01 |
| 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 | 24.350 - 1.800 |
| R-factor | 0.152 |
| Rwork | 0.150 |
| R-free | 0.18800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jmk |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.492 |
| 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 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.060 | 0.300 |
| Number of reflections | 26374 | |
| <I/σ(I)> | 32.7 | 4.1 |
| Completeness [%] | 99.4 | 93.8 |
| Redundancy | 7.8 |
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 |
