2Y5J
Crystal structure of Burkholderia cenocepacia dihydropteroate synthase.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2009-08-06 |
Detector | RIGAKU CCD |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 73.952, 89.433, 87.596 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 56.990 - 2.330 |
R-factor | 0.21063 |
Rwork | 0.207 |
R-free | 0.27403 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aj2 |
RMSD bond length | 0.008 |
RMSD bond angle | 2.160 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 57.280 | 2.480 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.120 | 0.360 |
Number of reflections | 12564 | |
<I/σ(I)> | 10 | 2.4 |
Completeness [%] | 99.5 | 97.1 |
Redundancy | 6.7 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.8 | RESERVOIR CONDITIONS 0.3 M TRIS/HCL PH8, 10% PEG 8000. PROTEIN SOLUTION BCDHPS AT 7.5 MGML-1, 2MM SULPHADOXINE, 50MM TRIS/HCL PH7.5, 250 MM NACL., pH 7.8 |