6P7K
Structure of HMG-CoA reductase from Burkholderia cenocepacia
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2016-05-28 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 141.485, 141.485, 122.967 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.312 - 1.722 |
R-factor | 0.1504 |
Rwork | 0.150 |
R-free | 0.16860 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6dio |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.730 |
High resolution limit [Å] | 1.720 | 5.880 | 1.720 |
Rmerge | 0.114 | 0.032 | 1.128 |
Rmeas | 0.117 | 0.033 | 1.211 |
Rpim | 0.026 | 0.007 | 0.401 |
Total number of observations | 1480729 | ||
Number of reflections | 76515 | 2152 | 1671 |
<I/σ(I)> | 8.6 | ||
Completeness [%] | 99.6 | 99.6 | 88.3 |
Redundancy | 19.4 | 19.9 | 6.4 |
CC(1/2) | 0.993 | 0.612 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277 | 0.2 M potassium acetate, pH 7.5, 20 g dL-1 PEG 3,350 |