4IEN
Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-08-24 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9537 |
Spacegroup name | P 21 3 |
Unit cell lengths | 152.520, 152.520, 152.520 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.950 - 2.000 |
R-factor | 0.16791 |
Rwork | 0.167 |
R-free | 0.19449 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vpm |
RMSD bond length | 0.026 |
RMSD bond angle | 2.590 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CCP4 |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.950 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.229 | |
Number of reflections | 79721 | |
Completeness [%] | 100.0 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 290 | 100mM Tris pH8.5, 2M ammonium Phosphate, 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 290K |