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