2QH1
Structure of TA289, a CBS-rubredoxin-like protein, in its Fe+2-bound state
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-03-20 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 58.806, 63.031, 97.474 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.670 - 2.000 |
R-factor | 0.202 |
Rwork | 0.202 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pvm |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.081 | 0.340 |
Number of reflections | 24893 | |
<I/σ(I)> | 52.7 | 13.6 |
Completeness [%] | 98.8 | 97.4 |
Redundancy | 10 | 10.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 298 | crystals were grown in a 1:1 solution of protein to resevoir containing 0.1 M Tris HCl (pH 7.8), 0.2 M ammonium formate, 20 % PEG 3350, and 8 % glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K |