6SYN
Crystal structure of Y. pestis penicillin-binding protein 3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-01-16 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.54178 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 40.860, 104.950, 110.420 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.000 - 2.630 |
R-factor | 0.2118 |
Rwork | 0.208 |
R-free | 0.27300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4bjp |
RMSD bond length | 0.003 |
RMSD bond angle | 1.388 |
Data reduction software | MOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 36.000 | 2.740 |
High resolution limit [Å] | 2.630 | 2.630 |
Rmerge | 0.122 | 0.234 |
Rmeas | 0.153 | 0.312 |
Rpim | 0.097 | 0.203 |
Number of reflections | 14613 | 1663 |
<I/σ(I)> | 7.8 | 3.9 |
Completeness [%] | 98.7 | 93.8 |
Redundancy | 3.9 | 3.1 |
CC(1/2) | 0.971 | 0.652 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 296 | 0.2 uL of protein (in 20 mM Tris-HCl pH 7.5 150 mM NaCl and 2 mM carbenicillin) at 6.7 mg/ml and 0.2 uL of precipitant (0.2 M magnesium acetate, 0.1 M sodium cacodylate pH 6.5 and 20% PEG 8000) |