5C9G

Crystal Structure of a Putative enoyl-CoA hydratase/isomerase family protein from Hyphomonas neptunium

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2014-03-24
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	63.479, 128.120, 209.646
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.100
R-factor	0.2
Rwork	0.198
R-free	0.23210
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4olq
RMSD bond length	0.011
RMSD bond angle	1.489
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0107)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.000	40.000	2.140
High resolution limit [Å]	2.100	5.700	2.100
Rmerge	0.135	0.053
Rmeas	0.140	0.057
Rpim	0.055	0.020	0.472
Total number of observations	726544
Number of reflections	98973
<I/σ(I)>	4.8
Completeness [%]	97.7	99.9	95.2
Redundancy	7.3	7.6	6.9
CC(1/2)		0.999	0.747

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	289	0.2 ul of 17.6 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of (the JCSG+ condition #G8) 0.15M DL-Malic acid, 19% PEG 3350 and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci).