4WD2
Crystal structure of an aromatic amino acid aminotransferase from Burkholderia cenocepacia J2315
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-08-25 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 1 2 |
Unit cell lengths | 59.220, 59.220, 200.270 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.647 - 1.950 |
R-factor | 0.1183 |
Rwork | 0.116 |
R-free | 0.15140 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3tat |
RMSD bond length | 0.005 |
RMSD bond angle | 0.893 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.5.7) |
Refinement software | PHENIX ((phenix.refine: dev_1779)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.000 | |
High resolution limit [Å] | 1.950 | 8.720 | 1.950 |
Rmerge | 0.090 | 0.031 | 0.346 |
Rmeas | 0.095 | 0.033 | 0.387 |
Total number of observations | 292285 | ||
Number of reflections | 29633 | 385 | 1986 |
<I/σ(I)> | 22.52 | 61.61 | 4.72 |
Completeness [%] | 99.1 | 98.2 | 90.9 |
Redundancy | 9.86 | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 290 | Rigaku Reagents JCSG+ screen d1: 24% PEG 1500, 20% glycerol; BuceA.01471.a.B1.PS01824 at 20 mg/ml + 2.5mM pyridoxal phosphate; di rect cryo; tray 257500 d1, puck zba1-4 |