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 |
