1ODF
Structure of YGR205w protein.
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 | 2001-04-15 |
Detector | MARRESEARCH |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 64.850, 64.850, 140.130 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.250 |
R-factor | 0.2063 |
Rwork | 0.206 |
R-free | 0.26000 * |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.195 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE/RESOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.320 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.055 | 0.499 |
Total number of observations | 94854 * | |
Number of reflections | 14707 | |
<I/σ(I)> | 33.2 | 3.9 |
Completeness [%] | 98.9 | 98.4 |
Redundancy | 6.4 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8 * | 18 * | 2.4M AMMONIUM SULFATE, 0.1M NA CITRATE PH5.6, pH 6.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 25 (mM) | pH8 |
3 | 1 | reservoir | ammonium sulfate | 1.9 (M) | |
4 | 1 | reservoir | sodium acetate | 0.1 (M) | pH4.5 |