1Q7C
The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR571 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-02-05 |
Detector | ENRAF-NONIUS |
Wavelength(s) | 1.5418 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 75.857, 95.857, 131.617 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 65.800 - 2.500 |
R-factor | 0.2187 |
Rwork | 0.215 |
R-free | 0.25200 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.170 * |
Data reduction software | SAINT |
Data scaling software | SAINT |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.800 | 2.610 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.057 * | 0.174 * |
Total number of observations | 172466 * | |
Number of reflections | 17095 | 2163 * |
Completeness [%] | 100.0 | 100 |
Redundancy | 10.1 * | 7.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.6 * | VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Tris-HCl | 20 (mM) | pH7.6 |
2 | 1 | drop | 50 (mM) | ||
3 | 1 | drop | dithiothreitol | 1 (mM) | |
4 | 1 | drop | EDTA | 1 (mM) | |
5 | 1 | drop | protein | 5 (mg/ml) | |
6 | 1 | reservoir | PEG1000 | 20 (%) | |
7 | 1 | reservoir | calcium acetate | 0.2 (M) | |
8 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH9.0 |