3AFM
Crystal structure of aldose reductase A1-R responsible for alginate metabolism
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-19 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 106.215, 106.215, 70.449 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 31.180 - 1.650 |
| R-factor | 0.17746 |
| Rwork | 0.176 |
| R-free | 0.20447 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1spx |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.964 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.710 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.051 | 0.401 |
| Number of reflections | 55401 | |
| <I/σ(I)> | 15.6 | 4.99 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 15.2 | 14.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.4 | 293 | 85mM tris-hydrochloride, 170mM lithium sulphate, 25.5% PEG 4000, 15% glycerol, pH 8.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
