4EFQ
Bombyx mori lipoprotein 7 - platinum derivative at 1.94 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X12 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-23 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.071 |
| Spacegroup name | P 1 |
| Unit cell lengths | 41.806, 49.785, 54.958 |
| Unit cell angles | 93.17, 94.87, 102.86 |
Refinement procedure
| Resolution | 54.600 - 1.940 |
| R-factor | 0.18675 |
| Rwork | 0.185 |
| R-free | 0.22665 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4efp |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.694 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | Auto-Rickshaw (MR protocol) |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.600 | 2.010 |
| High resolution limit [Å] | 1.940 | 1.940 |
| Rmerge | 0.068 | 0.153 |
| Number of reflections | 29990 | |
| <I/σ(I)> | 25.2 | 4.98 |
| Completeness [%] | 94.2 | 75 |
| Redundancy | 3.7 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 0.1 M HEPES buffer, 22% PEG 3350, 200 mM KSCN, 2.0 mM K2PtCl6, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
