1WLU
Crystal structure of TT0310 protein from Thermus thermophilus HB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44B2 |
Synchrotron site | SPring-8 |
Beamline | BL44B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-05-25 |
Detector | MARRESEARCH |
Wavelength(s) | 1.00 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 76.804, 76.804, 155.701 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.450 |
R-factor | 0.188 |
Rwork | 0.188 |
R-free | 0.19400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 1.100 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.490 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.061 | 0.635 |
Number of reflections | 41591 | |
<I/σ(I)> | 13 | 4.8 |
Completeness [%] | 100.0 | 100 |
Redundancy | 19.2 | 14.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7.5 | 18 * | MPD, sodium citrate, HEPES-NaOH, pH 7.5, Microbatch, temperature 295.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 30.0 (mg/ml) | |
2 | 1 | 1 | 50 (mM) | ||
3 | 1 | 1 | Tris-HCl | 20 (mM) | pH8.0 |
4 | 1 | 1 | MPD | 30 (%(v/v)) | |
5 | 1 | 1 | sodium citrate | 0.2 (M) | |
6 | 1 | 1 | HEPES-NaOH | 0.1 (M) | pH7.5 |