5VAW
Fusion of Maltose-binding Protein and PilA from Acinetobacter baumannii AB5075
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-03-08 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.557, 103.040, 56.195 |
| Unit cell angles | 90.00, 98.95, 90.00 |
Refinement procedure
| Resolution | 29.208 - 1.690 |
| R-factor | 0.2103 |
| Rwork | 0.209 |
| R-free | 0.24160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4xa2 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.610 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.31) |
| Phasing software | PHASER (2.6.0) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.210 | 29.210 | 1.720 |
| High resolution limit [Å] | 1.690 | 9.100 | 1.690 |
| Rmerge | 0.065 | 0.025 | 1.710 |
| Rmeas | 0.074 | 0.028 | 2.136 |
| Rpim | 0.035 | 0.013 | 1.261 |
| Total number of observations | 194591 | 1440 | 4091 |
| Number of reflections | 47148 | ||
| <I/σ(I)> | 11.1 | 50.1 | 0.5 |
| Completeness [%] | 95.0 | 97.1 | 63.3 |
| Redundancy | 4.1 | 4.4 | 2.5 |
| CC(1/2) | 0.999 | 0.999 | 0.277 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 0.1M MES/imidazole pH6.5, 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD, 0.02 M sodium L-glutamate, 0.02M DL-alanine, 0.02M glycine, 0.02M DL-lysine HCl, 0.02M DL-serine |
