1WEH

Crystal structure of the conserved hypothetical protein TT1887 from Thermus thermophilus HB8

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B1
Synchrotron site	SPring-8
Beamline	BL26B1
Temperature [K]	100
Detector technology	CCD
Collection date	2004-03-20
Detector	MARRESEARCH
Wavelength(s)	0.9792, 0.9794, 0.9742
Spacegroup name	C 2 2 21
Unit cell lengths	40.663, 129.821, 119.852
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.980 - 1.800
R-factor	0.185
Rwork	0.185
R-free	0.22300
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.860
High resolution limit [Å]	1.800	1.800
Number of reflections	29939
Completeness [%]	99.9	99.2
Redundancy	9.87354

Crystallization Conditions

crystal ID	method	pH	temperature	details
1