3BF4

Crystal structure of an ethd-like protein (reut_b5694) from ralstonia eutropha jmp134 at 2.10 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.1
Synchrotron site	ALS
Beamline	8.2.1
Temperature [K]	100
Detector technology	CCD
Collection date	2007-11-01
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9795, 0.9184, 0.9796
Spacegroup name	P 43 21 2
Unit cell lengths	74.540, 74.540, 98.870
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.761 - 2.100
R-factor	0.179
Rwork	0.178
R-free	0.21200
Structure solution method	MAD
RMSD bond length	0.013
RMSD bond angle	1.539
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHELX
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.761	29.761	2.170
High resolution limit [Å]	2.100	4.510	2.100
Rmerge	0.102	0.038	0.653
Number of reflections	16887	2977	2793
<I/σ(I)>	9.75	24.4	2.1
Completeness [%]	98.8	93.9	95.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	NANODROP, 15.0% Glycerol, 8.5% Isopropanol, 17.0% PEG 4000, 0.1M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K