1HV9
STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1999-04-06 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | H 3 2 |
Unit cell lengths | 104.500, 104.500, 648.200 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.250 - 2.100 |
R-factor | 0.211 |
Rwork | 0.211 |
R-free | 0.24800 |
Structure solution method | MIR |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.250 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.136 * | 0.233 |
Total number of observations | 495967 * | |
Number of reflections | 91622 * | |
<I/σ(I)> | 9.7 | 1.62 |
Completeness [%] | 98.0 * | 82.2 |
Redundancy | 5 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.4 | 293 | MES, ammonium sulfate, magnesium chloride, cobalt chloride, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8.3 (mg/ml) | |
2 | 1 | drop | UDP-GlcNAc | 14 (mM) | |
3 | 1 | drop | 28 (mM) | ||
4 | 1 | drop | 19 (mM) | ||
5 | 1 | reservoir | ammonium sulfate | 1.65 (M) | |
6 | 1 | reservoir | MES | 50 (mM) | |
7 | 1 | reservoir | 2-10 (mM) |