1V8D

Crystal structure of the conserved hypothetical protein TT1679 from Thermus thermophilus

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	100
Detector technology	CCD
Collection date	2003-03-08
Detector	MARRESEARCH
Wavelength(s)	0.9796, 0.9799, 0.9819, 0.9744
Spacegroup name	C 1 2 1
Unit cell lengths	102.799, 115.224, 75.270
Unit cell angles	90.00, 129.76, 90.00

Refinement procedure

Resolution	34.550 - 2.160
R-factor	0.189
Rwork	0.189
R-free	0.24900
Structure solution method	MAD
RMSD bond length	0.028
RMSD bond angle	2.400
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]	50.000	2.230
High resolution limit [Å]	2.150	2.150
Rmerge	0.044	0.095
Number of reflections	32472
<I/σ(I)>	17.3
Completeness [%]	93.1	73
Redundancy	2.4	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	PEG3350, MPD, Sodium Thiocyanate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	7	293	PEG3350, MPD, Sodium Thiocyanate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K