4PW0
Alpha/beta hydrolase fold protein from Chitinophaga pinensis
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 | 2014-03-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 62 |
| Unit cell lengths | 110.380, 110.380, 59.184 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.200 - 1.480 |
| R-factor | 0.105 |
| Rwork | 0.103 |
| R-free | 0.13330 |
| Structure solution method | SAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.662 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 37.200 | 50.000 | 1.510 |
| High resolution limit [Å] | 1.480 | 4.020 | 1.480 |
| Rmerge | 0.080 | 0.046 | 0.621 |
| Number of reflections | 133991 | ||
| <I/σ(I)> | 12.5 | 1.86 | |
| Completeness [%] | 99.9 | 99 | 99.9 |
| Redundancy | 5.1 | 5.2 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 297 | 3 M NaCl, 0.1 M Tris-HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
