4MF4
Crystal structure of a HpcH/Hpal aldolase/citrate lyase family protein from Burkholderia cenocepacia J2315
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-08-14 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9786 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 74.110, 116.480, 161.660 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.950 - 2.000 |
R-factor | 0.16702 |
Rwork | 0.165 |
R-free | 0.21254 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dxe |
RMSD bond length | 0.013 |
RMSD bond angle | 1.560 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.075 | 0.448 |
Number of reflections | 95110 | |
<I/σ(I)> | 21.7 | 4.15 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6 | 6.15 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | JCSG+a9: 20% PEG3350, 0.2M AmCl, VAPOR DIFFUSION, SITTING DROP, temperature 289K |