1DO2
TRIGONAL CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICHIA COLI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-06-15 |
Detector | MARRESEARCH |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 201.777, 201.777, 171.628 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 4.000 |
R-factor | 0.229 |
Rwork | 0.229 |
R-free | 0.28500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HSLU FROM HSLU IN HSLVU CRYSTALS |
RMSD bond length | 0.004 |
RMSD bond angle | 0.900 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 4.070 |
High resolution limit [Å] | 4.000 | 4.000 |
Rmerge | 0.105 | 0.337 |
Total number of observations | 224179 * | |
Number of reflections | 32750 | |
Completeness [%] | 95.8 | 96.5 |
Redundancy | 6 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | drop consists of equal volume of protein and reservoir solutions in Buffer B * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 16 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | Buffer B |
3 | 1 | drop | EDTA | 1 (mM) | Buffer B |
4 | 1 | drop | 1 (mM) | Buffer B | |
5 | 1 | reservoir | sodium cacodylate | 100 (mM) | |
6 | 1 | reservoir | glycerol | 15 (%) | |
7 | 1 | reservoir | PEG8000 | 10.5 (%) | |
8 | 1 | reservoir | ammonium sulfate | 500 (mM) |