2CVE

Crystal structure of a conserved hypothetical protein TT1547 from thermus thermophilus HB8

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	100
Detector technology	CCD
Collection date	2003-05-28
Detector	MAR CCD 165 mm
Wavelength(s)	1.00000
Spacegroup name	C 2 2 21
Unit cell lengths	53.670, 76.050, 102.110
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.010 - 1.600
R-factor	0.212
Rwork	0.212
R-free	0.23800
Structure solution method	MAD
RMSD bond length	0.025
RMSD bond angle	1.600
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.660
High resolution limit [Å]	1.600	1.600
Rmerge	0.037	0.189
Number of reflections	27824
<I/σ(I)>	42.3	7.84
Completeness [%]	99.5	96.9
Redundancy	5.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	293	0.8M Sodium/Potassium Tartrate, 0.5% PEG MME 5000, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	8.5	293	0.8M Sodium/Potassium Tartrate, 0.5% PEG MME 5000, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	8.5	293	0.8M Sodium/Potassium Tartrate, 0.5% PEG MME 5000, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K