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 |