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 |
