6D5K
Structure of Human ATP:Cobalamin Adenosyltransferase bound to ATP, and Adenosylcobalamin
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] | 298 |
Detector technology | PIXEL |
Collection date | 2017-06-08 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.5498 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 112.252, 112.252, 117.993 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 48.607 - 2.850 |
R-factor | 0.1957 |
Rwork | 0.192 |
R-free | 0.23940 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2idx |
Data reduction software | XDS |
Data scaling software | Aimless (3.24) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.610 | 48.610 | 2.810 |
High resolution limit [Å] | 2.680 | 8.900 | 2.680 |
Rmerge | 0.220 | 0.053 | 5.164 |
Rmeas | 0.232 | 0.056 | 5.458 |
Rpim | 0.074 | 0.018 | 1.752 |
Total number of observations | 242325 | ||
Number of reflections | 24504 | 754 | 3214 |
<I/σ(I)> | 7.6 | ||
Completeness [%] | 99.9 | 99.3 | 99.5 |
Redundancy | 9.9 | 9.4 | 9.6 |
CC(1/2) | 0.997 | 0.998 | 0.188 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 19% PEG 3350, 0.2 M MgSO4, 10 % glycerol |