1J27

Crystal structure of a hypothetical protein, TT1725, from Thermus thermophilus HB8 at 1.7A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Spacegroup name	C 2 2 21
Unit cell lengths	62.533, 68.388, 58.851
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	21.480 - 1.700
R-factor	0.178
Rwork	0.178
R-free	0.21800
Structure solution method	MAD
RMSD bond length	0.020
RMSD bond angle	24.300 *
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	1.700	1.700 *
Rmerge	0.028 *	0.097 *
Total number of observations	71421 *
Number of reflections	15362
Completeness [%]	98.7 *	89.6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5 *	20 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	1.9 (mg/ml)
2	1	drop	Tris	10 (mM)	pH8.5
3	1	drop	PEG3350	2.5 (%)
4	1	drop	sodium sulfate	75 (mM)