3B96

Structural Basis for Substrate Fatty-Acyl Chain Specificity: Crystal Structure of Human Very-Long-Chain Acyl-CoA Dehydrogenase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Temperature [K]	93
Detector technology	IMAGE PLATE
Collection date	2006-05-14
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5419
Spacegroup name	C 2 2 21
Unit cell lengths	74.616, 107.879, 149.776
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.690 - 1.910
R-factor	0.162
Rwork	0.159
R-free	0.21600
Structure solution method	MIRAS
RMSD bond length	0.014
RMSD bond angle	1.353
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE (2.05)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.980
High resolution limit [Å]	1.910	4.110	1.910
Rmerge	0.079	0.042	0.532
Number of reflections	46776
<I/σ(I)>	15.2
Completeness [%]	98.8	99.7	98.4
Redundancy	7.6	8.3	6.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	0.1 M HEPES, 17.6% PEG 2000, 0.047 M MgCl2, 5% glycerol, pH 7.5, vapor diffusion, hanging drop, temperature 298K
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	0.1 M HEPES, 17.6% PEG 2000, 0.047 M MgCl2, 5% glycerol, pH 7.5, vapor diffusion, hanging drop, temperature 298K
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	0.1 M HEPES, 17.6% PEG 2000, 0.047 M MgCl2, 5% glycerol, pH 7.5, vapor diffusion, hanging drop, temperature 298K