1ECF
ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 110 |
Detector technology | IMAGE PLATE |
Collection date | 1995-03-18 |
Detector | RIGAKU |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 116.900, 157.500, 106.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.175 |
Rwork | 0.175 |
R-free | 0.23000 |
Structure solution method | MOLECULAR REPLACEMENT AND SIR PHASES FROM SEMET PROTEIN |
Starting model (for MR) | 1gph |
RMSD bond length | 0.011 * |
RMSD bond angle | 1.730 * |
Data reduction software | HKL ((DENZO)) |
Data scaling software | HKL |
Phasing software | SHARP |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.041 | 0.225 |
Total number of observations | 268969 * | |
Number of reflections | 65480 | |
<I/σ(I)> | 24.1 | 4.5 |
Completeness [%] | 98.2 | 92.7 |
Redundancy | 4.1 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.5 * | 20 * | pH 5.6 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | PEG3350 | 15 (%(w/v)) | |
3 | 1 | reservoir | 2-propanol | 5 (%) | |
4 | 1 | reservoir | PIPES | 100 (mM) | |
5 | 1 | reservoir | 4 (mM) |