2DJW

Crystal structure of TTHA0845 from Thermus thermophilus HB8

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B2
Synchrotron site	SPring-8
Beamline	BL26B2
Temperature [K]	100
Detector technology	CCD
Collection date	2004-11-08
Detector	RIGAKU JUPITER 210
Wavelength(s)	1.0000
Spacegroup name	P 32
Unit cell lengths	95.883, 95.883, 119.010
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.400
R-factor	0.25198
Rwork	0.250
R-free	0.29351
Structure solution method	MAD, MOLECULAR REPLACEMENT
Starting model (for MR)	This protein model solved by MAD
RMSD bond length	0.012
RMSD bond angle	1.394
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.040	0.304
Number of reflections	47780
<I/σ(I)>	37.4	6.6
Completeness [%]	99.9	100
Redundancy	6.3	6.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	277	8.35mg/mL Protein, 2% PEG3350, 20mM Zn(OAc)2, 10mM MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
1	VAPOR DIFFUSION, SITTING DROP	6.5	277	8.35mg/mL Protein, 2% PEG3350, 20mM Zn(OAc)2, 10mM MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
1	VAPOR DIFFUSION, SITTING DROP	6.5	277	8.35mg/mL Protein, 2% PEG3350, 20mM Zn(OAc)2, 10mM MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K