5AFD
Native structure of N-acetylneuramininate lyase (sialic acid aldolase) from Aliivibrio salmonicida
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-09-17 |
| Detector | MARRESEARCH |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 66.942, 86.280, 117.733 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.180 - 1.650 |
| R-factor | 0.16604 |
| Rwork | 0.164 |
| R-free | 0.20122 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f74 |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.196 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.140 | 1.740 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.040 | 0.580 |
| Number of reflections | 41377 | |
| <I/σ(I)> | 20.2 | 2.8 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.1 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 25% PEG 1500, 20% GLYCEROL |
