5HY2
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 | 2015-02-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97070 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 93.297, 72.750, 133.054 |
| Unit cell angles | 90.00, 92.22, 90.00 |
Refinement procedure
| Resolution | 41.500 - 2.600 |
| R-factor | 0.20403 |
| Rwork | 0.202 |
| R-free | 0.24123 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5hy0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.259 |
| 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] | 46.600 | 2.720 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Number of reflections | 27567 | |
| <I/σ(I)> | 14 | 2.1 |
| Completeness [%] | 99.9 | 99.1 |
| Redundancy | 7.5 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 281 | Protein was at 2.7 mg/mL with added atrazine; reservoir was 22% PEG 3350, 86 mM sodium acetate; drops were 150 nL protein plus 140 nL reservoir plus 10 nL microseeds. |
