1MN9
NDP kinase mutant (H122G) complex with RTP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-06-10 |
Detector | MARRESEARCH |
Wavelength(s) | 1.542 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 71.731, 71.731, 153.818 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.200 - 2.900 |
Rwork | 0.207 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.117 * | |
Total number of observations | 93018 * | |
Number of reflections | 10566 * | |
Completeness [%] | 99.1 | 99.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 291 | PEG 550, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | PEG550 MME | 13 (%) | |
2 | 1 | drop | Tris-HCl | 100 (mM) | pH7.5 |
3 | 1 | drop | 30 (mM) | ||
4 | 1 | drop | protein | 10 (mg/ml) | |
5 | 1 | drop | RTP | 20 (mM) | |
6 | 1 | reservoir | PEG550 MME | 26 (%) |