1IIC
Crystal Structure of Saccharomyces cerevisiae N-myristoyltransferase with Bound MyristoylCoA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Temperature [K] | 103 |
Detector technology | IMAGE PLATE |
Collection date | 2000-04-10 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 2 2 21 |
Unit cell lengths | 75.129, 97.060, 141.809 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.220 - 2.200 |
R-factor | 0.236 |
Rwork | 0.236 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2nmt |
RMSD bond length | 0.007 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.048 * | |
Total number of observations | 341253 * | |
Number of reflections | 48952 | |
<I/σ(I)> | 19.4 | 7 |
Completeness [%] | 91.7 | 79.59 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.4 | 20 * | PEG 4000, ammonium acetate, sodium cacodylate, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25 (mg/ml) | |
2 | 1 | reservoir | ammonium acetate | 0.1 (M) | |
3 | 1 | reservoir | sodium cacodylate | 0.1 (M) | pH6.4 |
4 | 1 | reservoir | PEG4000 | 20 (%) |