5HXU
Structure-function analysis of functionally diverse members of the cyclic amide hydrolase family of Toblerone fold enzymes
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 | 2014-02-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.28221 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 83.415, 83.415, 216.234 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.500 - 1.830 |
| R-factor | 0.21268 |
| Rwork | 0.211 |
| R-free | 0.25165 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bvq |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.729 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.700 | 1.870 |
| High resolution limit [Å] | 1.830 | 1.830 |
| Number of reflections | 67015 | |
| <I/σ(I)> | 22.2 | 3.5 |
| Completeness [%] | 98.1 | 81 |
| Redundancy | 26.6 | 20.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | Protein at 15 mg/mL; reservoir was 2.5 M ammonium sulfate with 10% (v/v) MMT buffer at pH 9; sitting drop setup with 150 nL plus 150 nL drops; crystals cryo-protected with AP/E core 150 basestock (Mobile 1, Australia). |
