3V9O
Crystal structure of Dihydroneopterin aldolase (BTH_I0291) from Burkholderia thailendensis bound to guanine.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-12-01 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97740 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 73.984, 73.984, 110.976 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.064 - 1.451 |
| R-factor | 0.1752 |
| Rwork | 0.174 |
| R-free | 0.20440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3o1k |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.812 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.480 |
| High resolution limit [Å] | 1.450 | 3.940 | 1.450 |
| Rmerge | 0.061 | 0.042 | 0.559 |
| Number of reflections | 27570 | ||
| <I/σ(I)> | 13.5 | ||
| Completeness [%] | 99.9 | 98.9 | 100 |
| Redundancy | 14.1 | 13.3 | 14.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 2 M ammonium sulfate, 0.2 M lithium sulfate, 0.1 M TRIS, SSGCID: ButhA.17925.a.A1 PW33456, VAPOR DIFFUSION, SITTING DROP, temperature 289K, pH 7.0 |
