2V0P
The Structure of Tap42 Alpha4 Subunit
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-05-01 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 44.633, 48.308, 71.960 |
Unit cell angles | 81.31, 87.94, 69.83 |
Refinement procedure
Resolution | 71.070 - 1.800 |
R-factor | 0.239 |
Rwork | 0.238 |
R-free | 0.25600 |
Structure solution method | SAD |
RMSD bond length | 0.019 |
RMSD bond angle | 1.558 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELX |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.050 | 0.460 |
Number of reflections | 49867 | |
<I/σ(I)> | 15.6 | 2.6 |
Completeness [%] | 96.4 | 96.4 |
Redundancy | 4.4 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | THE PROTEIN WAS CONCENTRATED TO 10 MG/ML BEFORE CRYSTALLIZATION. CRYSTALS WERE GROWN AT 20C USING THE HANGING DROP METHOD. ONE MICROLITRE OF PROTEIN WAS MIXED WITH AN EQUAL VOLUME OF CRYSTALLIZATION BUFFER: 20% (W/V) PEG 8000, 0.1 M SODIUM CACODYLATE PH 6.5, 0.2 M MAGNESIUM ACETATE AND 2MM DTT. CRYSTALS WERE OPTIMISED BY SEEDING. |