4EFR
Bombyx mori lipoprotein 7 (crystal form II) at 2.50 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 | 2011-05-09 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.949 |
| Spacegroup name | P 1 |
| Unit cell lengths | 35.100, 71.720, 105.120 |
| Unit cell angles | 78.79, 89.98, 75.79 |
Refinement procedure
| Resolution | 37.000 - 2.500 |
| R-factor | 0.2038 |
| Rwork | 0.201 |
| R-free | 0.28532 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4efp |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.983 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | Auto-Rickshaw (MR protocol) |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.000 | 2.560 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.043 | 0.147 |
| Number of reflections | 29884 | |
| <I/σ(I)> | 13.88 | 4.67 |
| Completeness [%] | 88.8 | 88.8 |
| Redundancy | 1.8 | 1.6 |
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, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
