5AED
A bacterial protein structure in glycoside hydrolase family 31
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04-1 |
Synchrotron site | Diamond |
Beamline | I04-1 |
Temperature [K] | 293 |
Detector technology | PIXEL |
Collection date | 2014-11-16 |
Detector | DECTRIS PILATUS 2M |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 78.710, 113.177, 111.720 |
Unit cell angles | 90.00, 109.23, 90.00 |
Refinement procedure
Resolution | 105.490 - 1.910 |
R-factor | 0.1697 |
Rwork | 0.168 |
R-free | 0.20134 |
Structure solution method | SAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.019 |
RMSD bond angle | 1.813 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | SHELX |
Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.060 | 1.940 |
High resolution limit [Å] | 1.910 | 1.910 |
Rmerge | 0.080 | 0.540 |
Number of reflections | 138269 | |
<I/σ(I)> | 7.9 | 2 |
Completeness [%] | 96.8 | 99.2 |
Redundancy | 2.8 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 293 | 25 MG/ML PROTEIN IN THE BUFFER OF 50 MM NAPO4 BUFFER PH 7.5 AND 250 MM NACL WAS MIXED 1:1 WITH THE PRECIPITANT COMPOSED OF 50-60% MPD, 0.1-0.15M CACL2 AND BIS-TRIS PH 6.5. TEMP: 20 C |