4UIA
Crystal structure of 3a in complex with tafCPB
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-01-29 |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 83.673, 83.673, 97.035 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 63.370 - 2.180 |
R-factor | 0.2189 |
Rwork | 0.216 |
R-free | 0.25140 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PREVIOUSLY SOLVED IN-HOUSE STRUCTURE |
RMSD bond length | 0.008 |
RMSD bond angle | 0.920 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Refinement software | BUSTER (2.11.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 83.740 | 2.250 |
High resolution limit [Å] | 2.180 | 2.180 |
Rmerge | 0.170 | 0.460 |
Number of reflections | 18470 | |
<I/σ(I)> | 7.9 | 3.3 |
Completeness [%] | 99.3 | 98.3 |
Redundancy | 4.5 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | THE PURIFIED PROTEIN WAS DISSOLVED IN 50 MM TRIS-HCL, PH 7.5 AND CONCENTRATED TO 11 MG/ML. 1 UL OF PROTEIN SOLUTION WAS EQUILIBRATED AGAINST 1 UL OF RESERVOIR SOLUTIONS CONTAINING 16-20% PEG3350, 100 MM MES PH 5.5 AND 50 MM ZNACETATE. |