5IZT
Crystal structure of a C-terminal proteolytic fragment of an outer surface protein from Borrelia burgdorferi
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-03-11 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 1 |
Unit cell lengths | 31.340, 54.030, 66.960 |
Unit cell angles | 101.44, 98.73, 85.00 |
Refinement procedure
Resolution | 27.405 - 1.900 |
R-factor | 0.1688 |
Rwork | 0.166 |
R-free | 0.21130 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yn7 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.770 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((dev_2356)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.950 |
High resolution limit [Å] | 1.900 | 8.500 | 1.900 |
Rmerge | 0.054 | 0.026 | 0.482 |
Number of reflections | 32761 | ||
<I/σ(I)> | 17.18 | 41.93 | 3.06 |
Completeness [%] | 97.7 | 95.7 | 96.3 |
Redundancy | 3.92 | ||
CC(1/2) | 0.998 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 290 | Microlytic MCSG 1 screen H3: 20% PEG 4000, 20% iso-Propanol, 100mM Na3-citrate pH 5.6; BobuA.18967.a.B2.PW37767 at 20mg/ml; cryo: 20% EG; tray 266029 h3; puck rgo9-7 |