3K1E
Crystal structure of odorant binding protein 1 (AaegOBP1) from Aedes aegypti
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12B |
Synchrotron site | NSLS |
Beamline | X12B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-27 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 34.248, 47.870, 69.082 |
Unit cell angles | 90.00, 96.61, 90.00 |
Refinement procedure
Resolution | 68.680 - 1.850 |
R-factor | 0.154 |
Rwork | 0.151 |
R-free | 0.21200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2erb |
RMSD bond length | 0.010 |
RMSD bond angle | 1.188 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.000 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Number of reflections | 19077 | |
<I/σ(I)> | 20.35 | 4.4 |
Completeness [%] | 99.6 | 98.9 |
Redundancy | 7.3 | 7.38 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 2 microliter drops, with equal volumes of protein at 50 mg/mL and reservoir solution containing 28% PEG 8000, 250 mM MgCl2, 50 mM Tris-HCl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |