6XD8
Crystal Structure of Peptidylprolyl Isomerase (PrsA) Fragment from Bacillus anthracis
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 | 2020-02-14 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 48.889, 107.344, 31.698 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.310 - 1.520 |
R-factor | 0.1722 |
Rwork | 0.170 |
R-free | 0.22190 |
Structure solution method | SAD |
RMSD bond length | 0.004 |
RMSD bond angle | 1.285 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.550 |
High resolution limit [Å] | 1.520 | 1.520 |
Rmerge | 0.061 | 0.723 |
Rmeas | 0.066 | 0.780 |
Rpim | 0.025 | 0.289 |
Number of reflections | 26434 | 1272 |
<I/σ(I)> | 28.5 | 2.9 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.1 | 7.2 |
CC(1/2) | 0.817 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 292 | Protein: 7.8 mg/ml, 0.01M Tris pH 8.3; Screen: Classics II (H11), 0.1M Potassium thiocyanate, 30% (w/v) PEG 2000 MME |