1I0H
CRYSTAL STRUCTURE OF THE E. COLI MANGANESE SUPEROXIDE DISMUTASE MUTANT Y174F AT 1.35 ANGSTROMS RESOLUTION.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 110 |
| Detector technology | AREA DETECTOR |
| Collection date | 1998-11-01 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9058 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.893, 46.017, 95.993 |
| Unit cell angles | 90.00, 98.40, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.350 |
| R-factor | 0.169 |
| Rwork | 0.170 |
| R-free | 0.19600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.015 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.370 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.027 | 0.071 |
| Total number of observations | 561459 * | |
| Number of reflections | 89109 | |
| <I/σ(I)> | 52.5 | 18.3 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 4.2 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | drop consists of 2 micro litter of protein solution in 0.1 M bicine plus 2 micro litter of reservoir solution * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 18-20 (mg/ml) | |
| 2 | 1 | drop | Bicine | 0.1 (M) | |
| 3 | 1 | reservoir | PEG6000 | 16-20 (%) | |
| 4 | 1 | reservoir | bicine | 0.1 (M) |
