4S1P
Shel_16390 protein, a putative SGNH hydrolase from Slackia heliotrinireducens
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-05-30 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.591, 67.023, 71.544 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.300 - 1.450 |
| R-factor | 0.1195 |
| Rwork | 0.118 |
| R-free | 0.15590 |
| Structure solution method | SAD |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.538 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXCD |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 35.300 | 50.000 | 1.480 |
| High resolution limit [Å] | 1.450 | 3.940 | 1.450 |
| Rmerge | 0.143 | 0.096 | 0.654 |
| Number of reflections | 35098 | ||
| <I/σ(I)> | 12.1 | 1.95 | |
| Completeness [%] | 98.9 | 98.5 | 88.9 |
| Redundancy | 6.2 | 6.5 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 289 | 0.1 M sodium acetate, 1.5 M lithium sulfate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
