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 |