2IDX
Structure of Human ATP:Cobalamin adenosyltransferase bound to ATP.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X26C |
Synchrotron site | NSLS |
Beamline | X26C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-08-09 |
Wavelength(s) | 1.0 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 111.238, 111.238, 115.526 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.500 |
R-factor | 0.2 |
Rwork | 0.197 |
R-free | 0.25100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rty |
RMSD bond length | 0.012 |
RMSD bond angle | 1.484 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.136 | 0.560 |
Number of reflections | 29063 | |
<I/σ(I)> | 9 | 2 |
Completeness [%] | 100.0 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 20% PEG 3350, 0.2 M MgSO4, 10% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 298K |