1NRK
YGFZ PROTEIN
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-BM |
Synchrotron site | APS |
Beamline | 17-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-04-12 |
Detector | MARRESEARCH |
Wavelength(s) | 1.000 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 151.000, 151.000, 68.000 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.800 |
R-factor | 0.19592 |
Rwork | 0.193 |
R-free | 0.25200 * |
Structure solution method | MAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.600 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.055 | 0.440 * |
Number of reflections | 21998 | 2412 * |
<I/σ(I)> | 22.4 | 2.1 |
Completeness [%] | 98.5 | 97.1 |
Redundancy | 4.9 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 295 | 0.1M Na Acetate, 30% Ammonium Sulfate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 30 (%sat) | |
3 | 1 | reservoir | sodium acetate | 0.1 (M) | pH4.5 |