5EDF
Crystal structure of the selenomethionine-substituted iron-regulated protein FrpD from Neisseria meningitidis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-03 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.293, 38.829, 165.670 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.200 - 1.400 |
| R-factor | 0.169 |
| Rwork | 0.168 |
| R-free | 0.19270 |
| Structure solution method | SAD |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.432 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.450 |
| High resolution limit [Å] | 1.400 | 3.020 | 1.400 |
| Rmerge | 0.047 | 0.034 | 0.319 |
| Total number of observations | 269990 | ||
| Number of reflections | 47065 | ||
| <I/σ(I)> | 13 | ||
| Completeness [%] | 94.2 | 99 | 80.9 |
| Redundancy | 5.7 | 6.7 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1M Tris-HCl, 20% (w/v) PEG 8000, 20% (v/v) PEG 400, and 0.1M MgCl2 |
