5H6U
Structure of alginate-binding protein AlgQ2 in complex with an alginate pentasaccharide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-05-22 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 46.107, 59.179, 82.724 |
| Unit cell angles | 84.62, 90.16, 87.99 |
Refinement procedure
| Resolution | 35.680 - 2.006 |
| R-factor | 0.2043 |
| Rwork | 0.201 |
| R-free | 0.26070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1j1n |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.041 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.053 | 0.157 |
| Number of reflections | 56452 | |
| <I/σ(I)> | 31.4 | 5.6 |
| Completeness [%] | 97.4 | 96.1 |
| Redundancy | 3.1 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293.15 | 25% PEG4000, 0.2 M calcium chloride, 0.1 M tris(hydroxymethyl)aminomethan-hydrochloride acid |
