1P48
REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2001-10-23 |
Detector | BRUKER PROTEUM R |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 107.800, 114.500, 73.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.21300 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | LSCALE ((Bruker Nonius)) |
Data scaling software | SAINT |
Phasing software | MOLREP ((CCP4)) |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.090 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.064 * | 0.189 * |
Total number of observations | 231529 * | |
Number of reflections | 61265 | |
Completeness [%] | 99.0 | 99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8 | 293 | PEG 8000, potassium chloride, HEPPS, pH 8.0, Batch, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 10 (mg/ml) | |
2 | 1 | 1 | PEG8000 | 13 (%) | |
3 | 1 | 1 | 0.25 (M) | ||
4 | 1 | 1 | HEPPS/KCH | 25 (mM) | pH8.0 |
5 | 1 | 1 | PEP | 3.5 (mM) | |
6 | 1 | 1 | 3.5 (mM) |