1HXT
OMPF PORIN MUTANT NQAAA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-01-01 |
Detector | MARRESEARCH |
Wavelength(s) | 0.992 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 117.084, 117.084, 51.344 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.400 |
R-factor | 0.213 * |
Rwork | 0.233 |
R-free | 0.28500 * |
Structure solution method | difference fourier |
RMSD bond length | 0.010 * |
RMSD bond angle | 0.033 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.079 | 0.310 |
Total number of observations | 53590 * | |
Number of reflections | 14853 | |
<I/σ(I)> | 7.5 | |
Completeness [%] | 93.1 | 93.5 |
Redundancy | 3.6 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | Pauptit, R.A., (1991) J. Mol. Biol., 218, 505. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 10 (mg/ml) | |
2 | 1 | 2 | PEG2000 | 10.5 (%) |