7RUT
Structure of Human ATP:Cobalamin Adenosyltransferase R190C bound to ATP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-11-15 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0332 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 77.151, 75.769, 95.844 |
Unit cell angles | 90.00, 91.30, 90.00 |
Refinement procedure
Resolution | 40.494 - 1.500 |
R-factor | 0.1516 |
Rwork | 0.150 |
R-free | 0.18450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2idx |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.900 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.060 | 1.072 |
Number of reflections | 176322 | 8753 |
<I/σ(I)> | 12.8 | |
Completeness [%] | 99.9 | |
Redundancy | 6.6 | |
CC(1/2) | 1.000 | 0.660 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 30% (v/v) 2-propanol, 100 mM Tris pH 8.5, and 30% (w/v) PEG 3350 |