2IXM
Structure of human PTPA
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-05-09 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.243, 70.410, 95.534 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 56.700 - 1.500 |
R-factor | 0.203 |
Rwork | 0.202 |
R-free | 0.22100 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.207 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELX |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 22.000 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.090 | 0.300 |
Number of reflections | 311889 | |
<I/σ(I)> | 13.7 | 5.9 |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.9 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | PTPA CRYSTALS WERE GROWN USING THE HANGING DROP METHOD AT 20C. 1UL OF PROTEIN (20 MG/ML) WAS MIXED WITH 1 UL OF PRECIPITANT (23% TO 28% PEG 4000, 0.2 M LITHIUM SULFATE, 0.1 M TRIS PH 7.0-8.5 AND 5 MM DTT) WERE EQUILIBRATED AGAINST 0.5 ML OF PRECIPITANT. LARGE PLATE CRYSTALS APPEARED IN 2 TO 3 DAYS. FOR CRYOPROTECTION 5% MPD WAS ADDED TO THE PRECIPITANT SOLUTION. |