1UAN

Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	93
Detector technology	CCD
Collection date	2002-02-05
Detector	MARRESEARCH
Wavelength(s)	0.9821, 0.9808, 0.9803, 0.9752
Spacegroup name	P 3 2 1
Unit cell lengths	107.134, 107.134, 98.617
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 * - 2.000
R-factor	0.20296
Rwork	0.201
R-free	0.24300 *
Structure solution method	MAD
RMSD bond length	0.022
RMSD bond angle	1.800 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.038 *	0.202 *
Total number of observations	406551 *
Number of reflections	44178 *
Completeness [%]	99.3 *	94.2 *
Redundancy	9.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.1	20 *	ammonium sulfate, sodium chloride, HEPES, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	30 (mg/ml)
2	1	reservoir	ammonium sulfate	1.6 (M)
3	1	reservoir	HEPES-HCl	100 (mM)	pH7.1
4	1	reservoir		100 (mM)