2EIS

X-ray structure of acyl-CoA hydrolase-like protein, TT1379, from Thermus thermophilus HB8

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2007-02-02
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9793
Spacegroup name	P 21 3
Unit cell lengths	105.675, 105.675, 105.675
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.260 - 2.100
R-factor	0.219
Rwork	0.219
R-free	0.23900
Structure solution method	MAD and MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.400
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.080	0.287
Number of reflections	23244
<I/σ(I)>	11.3
Completeness [%]	100.0	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.2	298	30% v/v Propylene Glycol, 4% v/v PEG 400, 20% v/v Glycerol, 0.1M Na3Citrate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K