6LNW
Crystal structure of accessory secretory protein 1,2 and 3 in Streptococcus pneumoniae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-04-20 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97915 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 101.158, 101.158, 196.851 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 42.940 - 2.900 |
R-factor | 0.1993 |
Rwork | 0.197 |
R-free | 0.24160 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5vae |
RMSD bond length | 0.009 |
RMSD bond angle | 1.298 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Number of reflections | 26531 | 2586 |
<I/σ(I)> | 12.25 | |
Completeness [%] | 99.8 | |
Redundancy | 4.7 | |
CC(1/2) | 0.991 | 0.833 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | 0.1 M Tris pH 8.0, 15% PEG 6000 |