5CFV
Fusion of Maltose-binding Protein and PilA from Acinetobacter nosocomialis M2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-06-28 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.034 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 173.883, 55.334, 49.670 |
Unit cell angles | 90.00, 91.52, 90.00 |
Refinement procedure
Resolution | 29.440 - 1.800 |
Rwork | 0.182 |
R-free | 0.22800 |
Structure solution method | MOLECULAR REPLACEMENT |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.9) |
Phasing software | PHASER (2.5.6) |
Refinement software | PHENIX (1.9-1692) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.440 | 29.440 | 1.840 |
High resolution limit [Å] | 1.800 | 9.010 | 1.800 |
Rmerge | 0.047 | 0.030 | 0.480 |
Rpim | 0.029 | 0.019 | 0.386 |
Total number of observations | 151005 | 1263 | 5010 |
Number of reflections | 42472 | ||
<I/σ(I)> | 15.4 | 37.9 | 1.8 |
Completeness [%] | 97.0 | 96 | 77.1 |
Redundancy | 3.6 | 3.4 | 2.5 |
CC(1/2) | 0.998 | 0.997 | 0.799 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 298 | Drops were set at a ratio of 2:1 mother-liquor to protein, at 10mg/ml protein concentration. The mother-liquor consisted of 0.1M Bicine/Trizma pH 8.0, 0.06M MgCl2, 0.06M CaCl2, 25% MPD, 25% PEG3350, 25% PEG400 |