7TPM
Structure of the outer-membrane lipoprotein carrier protein (LolA) from Borrelia burgdorferi
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-03-04 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0000 |
Spacegroup name | P 41 3 2 |
Unit cell lengths | 122.136, 122.136, 122.136 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.623 - 1.900 |
R-factor | 0.1927 |
Rwork | 0.191 |
R-free | 0.23120 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | SAD-phased structure of the same protein from a KI-soaked crystal |
RMSD bond length | 0.010 |
RMSD bond angle | 1.028 |
Data reduction software | XDS |
Data scaling software | Aimless (0.6.3) |
Phasing software | CRANK2 |
Refinement software | PHENIX (dev_3111) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 49.860 | 49.860 | 1.940 |
High resolution limit [Å] | 1.900 | 9.110 | 1.900 |
Rmerge | 0.145 | 0.065 | 2.391 |
Total number of observations | 488064 | 4502 | 32022 |
Number of reflections | 25182 | 299 | 1597 |
<I/σ(I)> | 12.5 | 35.1 | 1.5 |
Completeness [%] | 100.0 | 99.5 | 100 |
Redundancy | 19.4 | 15.1 | 20.1 |
CC(1/2) | 0.999 | 0.997 | 0.738 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 2 M sodium formate, 100 mM MES, 5% (w/v) PEG 5000 MME |