1WG0
Structural comparison of Nas6p protein structures in two different crystal forms
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-03-04 |
| Detector | RIGAKU |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.444, 68.629, 46.985 |
| Unit cell angles | 90.00, 108.95, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.530 |
| R-factor | 0.182 |
| Rwork | 0.179 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ixv |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.620 |
| High resolution limit [Å] | 2.530 | 2.530 |
| Rmerge | 0.095 | 0.191 |
| Number of reflections | 8677 | |
| <I/σ(I)> | 9.5 | |
| Completeness [%] | 98.7 | 93.8 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.7 | 298 | 15-20% PEG 4000, 0.1M MES, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
