1GY7
N77Y point mutant of S.Cerevisiae NTF2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 58.660, 83.870, 61.500 |
Unit cell angles | 90.00, 115.86, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.600 |
R-factor | 0.202 |
Rwork | 0.202 |
R-free | 0.22300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1oun |
RMSD bond length | 0.005 |
RMSD bond angle | 1.400 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.000 | 1.690 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.070 | 0.321 |
Total number of observations | 353243 * | |
Number of reflections | 66296 | |
<I/σ(I)> | 5.2 | 2 |
Completeness [%] | 94.0 | 69.5 |
Redundancy | 3.4 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 18 * | 100MM AMMONIUM ACETATE, PH 6.5 1.12M AMMONIUM SULPHATE(WELL),1.6M AMMONIUM SULPHATE(DROP) 7 MG/ML PROTEIN - SEE PAPER |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | ammonium acetate | 50 (mM) | pH6.5 |
2 | 1 | drop | ammonium sulfate | 0.8 (M) | |
3 | 1 | drop | protein | 7 (mg/ml) | |
4 | 1 | reservoir | ammonium acetate | 100 (mM) | pH6.5 |
5 | 1 | reservoir | ammonium sulfate | 1.12 (M) |