5HY4
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 | 2014-12-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.95370 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 92.762, 105.799, 299.127 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.700 - 2.560 |
| R-factor | 0.2311 |
| Rwork | 0.229 |
| R-free | 0.26343 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5hy0 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.522 |
| 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] | 46.700 | 2.600 |
| High resolution limit [Å] | 2.560 | 2.560 |
| Number of reflections | 95206 | |
| <I/σ(I)> | 12.5 | 1.8 |
| Completeness [%] | 99.5 | 98.9 |
| Redundancy | 7.5 | 7.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 281 | Protein was concentrated to 4.2 mg/mL; reservoir was 20% PEG 3350 and 0.2 M magnesium acetate at 8 C; drops were 150 nL protein plus 150 nL reservoir. |
