1IT3
Hagfish CO ligand hemoglobin
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 | 2000-10-23 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 44.973, 150.636, 51.943 |
Unit cell angles | 90.00, 106.37, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.100 |
R-factor | 0.195 * |
Rwork | 0.196 |
R-free | 0.28300 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1f5o |
RMSD bond length | 0.008 |
RMSD bond angle | 1.100 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.070 * | 0.181 |
Total number of observations | 73549 * | |
Number of reflections | 32410 | |
<I/σ(I)> | 10.9 | |
Completeness [%] | 83.2 * | 63.9 |
Redundancy | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 6.5 | 27 * | PEG 4000, Tris-Buffer, pH 6.5, SMALL TUBES, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | PEG4000 | 21 (%) | |
2 | 1 | 1 | glycerol | 10 (%) | |
3 | 1 | 1 | Bis-Tris-HCl | 50 (mM) | pH6.5 |
4 | 1 | 1 | 2-mercaptoethanol | 0.020 (mM) | |
5 | 1 | 1 | 100 (mM) | ||
6 | 1 | 1 | protein | 1.5 (%) |