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 |