3NRF
Crystal structure of an apag protein (PA1934) from pseudomonas aeruginosa pao1 at 1.50 A resolution
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-05-12 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 0.91837,0.97936,0.97922 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 69.343, 96.491, 61.788 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.178 - 1.500 |
R-factor | 0.186 |
Rwork | 0.184 |
R-free | 0.22200 |
Structure solution method | MAD |
RMSD bond length | 0.016 |
RMSD bond angle | 1.697 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.15) |
Phasing software | SHELX |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.178 | 1.540 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 32823 | |
<I/σ(I)> | 8.5 | 1.6 |
Completeness [%] | 98.4 | 95.8 |
Redundancy | 4.4 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 40.000000000% MPD, 5.000000000% PEG-8000, 0.1M Cacodylate pH 6.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K |