1J3M

Crystal structure of the conserved hypothetical protein TT1751 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]	100
Detector technology	CCD
Collection date	2002-02-04
Detector	MARRESEARCH
Wavelength(s)	0.9804, 0.9808, 0.9825, 0.9720
Spacegroup name	P 1 21 1
Unit cell lengths	41.603, 78.811, 44.688
Unit cell angles	90.00, 116.64, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.19694
Rwork	0.194
R-free	0.25884
Structure solution method	MAD
RMSD bond length	0.024
RMSD bond angle	2.150
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]	50.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.036	0.138
Number of reflections	16980
<I/σ(I)>	16.8
Completeness [%]	97.9	83.8
Redundancy	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microbatch Crystallization	5.6	293	PEGMME 5000, Ammonium Sulfate, pH 5.6, Microbatch Crystallization, temperature 293K