2H8V
Structure of empty Pheromone Binding Protein ASP1 from the Honeybee Apis mellifera L
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-12-14 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.934 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 76.098, 85.997, 50.839 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.600 |
R-factor | 0.21818 |
Rwork | 0.210 |
R-free | 0.26625 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.368 |
Data scaling software | SCALA |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.667 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 4835 | |
Completeness [%] | 99.2 | 99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.9 | 298 | 200 nL of a 40 mg/mL protein solution in Tris 10 mM, NaCl 25 mM, mixed with 100 nL of 2.2 M ammonium sulfate, 0.2 M ammonium iodide, pH 5.9, VAPOR DIFFUSION, SITTING DROP, temperature 298K |