3WCT
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Oxygenated form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-06 |
Detector | Bruker DIP-6040 |
Wavelength(s) | 0.9000 |
Spacegroup name | P 63 |
Unit cell lengths | 108.556, 108.556, 193.552 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.020 - 2.400 |
R-factor | 0.216 |
Rwork | 0.216 |
R-free | 0.26400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1yhu |
RMSD bond length | 0.007 |
RMSD bond angle | 1.100 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 50516 | |
<I/σ(I)> | 28.6 | 6.7 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.7 | 11.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 13-18% PEG 3350, 0-5mM Ca acetate/Mg acetate, 100mM HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |