1HIY
Binding of nucleotides to NDP kinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LURE BEAMLINE DW32 |
Synchrotron site | LURE |
Beamline | DW32 |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Wavelength(s) | 0.97 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 71.620, 71.620, 153.800 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.600 |
R-factor | 0.22 |
Rwork | 0.220 |
R-free | 0.32500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1kdn |
RMSD bond length | 0.014 |
RMSD bond angle | 1.680 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 15.000 |
High resolution limit [Å] | 2.200 |
Rmerge | 0.049 |
Number of reflections | 23760 |
Completeness [%] | 99.7 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 * | METHOD: HANGING DROP IN DROP: 5MG/ML PROTEIN, 50 MM TRIS HCL PH8.5, 8.5MM 3'-AMINO-ADP,15-16% PEG550, 20MM MGCL2 IN WELL: 30-32% PEG550, 50MM TRISHCL PH8.5., pH 8.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | ADP | 17 (mM) | |
2 | 1 | drop | protein | 5 (mg/ml) | |
3 | 1 | drop | 20 (mM) | ||
4 | 1 | drop | Tris-HCl | 50 (mM) | |
5 | 1 | drop | PEG550 | 15-16 (%) |