6JHH
Crystal structure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose
Replaces: 5WVSExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL18U1 |
| Synchrotron site | SSRF |
| Beamline | BL18U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-09-21 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97776 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 72.822, 78.803, 116.348 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.802 - 2.025 |
| R-factor | 0.1702 |
| Rwork | 0.167 |
| R-free | 0.23310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2e8y |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.897 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.025 | 2.025 |
| Rmerge | 0.106 | 0.499 |
| Number of reflections | 40754 | 2298 |
| <I/σ(I)> | 16.3 | 3.33 |
| Completeness [%] | 99.5 | 98.3 |
| Redundancy | 6.5 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.08M calcium chloride, 0.1M MES, 22% PEG 3350, 0.7% beta-OG, pH 6.5 |
