2E67

Crystal structure of the hypothetical protein TTHB029 from Thermus thermophilus HB8

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B2
Synchrotron site	SPring-8
Beamline	BL26B2
Temperature [K]	100
Detector technology	CCD
Collection date	2004-11-05
Detector	RIGAKU JUPITER 210
Wavelength(s)	0.900
Spacegroup name	H 3 2
Unit cell lengths	202.006, 202.006, 345.294
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.900
R-factor	0.22109
Rwork	0.219
R-free	0.25934
Structure solution method	MAD
RMSD bond length	0.017
RMSD bond angle	1.863
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	SOLVE
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	3.000
High resolution limit [Å]	2.900	2.900
Rmerge	0.070	0.354
Number of reflections	56883
Completeness [%]	100.0	100
Redundancy	5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	295	20mM Na Acetate buffer, 300mM Mg Formate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K
1	VAPOR DIFFUSION, SITTING DROP	5	295	20mM Na Acetate buffer, 300mM Mg Formate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K
1	VAPOR DIFFUSION, SITTING DROP	5	295	20mM Na Acetate buffer, 300mM Mg Formate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K