6VJ2
3.10 Angstrom Resolution Crystal Structure of Foldase Protein (PrsA) from Lactococcus lactis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-08-16 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 81.513, 117.609, 149.310 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.400 - 3.100 |
R-factor | 0.2364 |
Rwork | 0.234 |
R-free | 0.28970 |
Structure solution method | SAD |
RMSD bond length | 0.004 |
RMSD bond angle | 1.241 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.150 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.122 | 0.776 |
Rmeas | 0.137 | 0.867 |
Rpim | 0.061 | 0.381 |
Number of reflections | 26817 | 1306 |
<I/σ(I)> | 13.7 | 2.1 |
Completeness [%] | 99.9 | 100 |
Redundancy | 4.9 | 5 |
CC(1/2) | 0.787 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 292 | Protein: 6.4 mg/ml, 0.01M Tris HCl (pH 8.3); Reservoir (PEGs II screen, B6): 0.1M HEPES (pH 7.5), 20% (w/v) PEG 1500 |