1UFI

Crystal structure of the dimerization domain of human CENP-B

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	2002-12-02
Detector	MARRESEARCH
Wavelength(s)	0.9781, 0.9824, 0.9803, 0.9808
Spacegroup name	P 21 21 21
Unit cell lengths	43.707, 48.955, 100.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 1.650
R-factor	0.23596
Rwork	0.232
R-free	0.30900 *
Structure solution method	MAD
RMSD bond length	0.033
RMSD bond angle	1.747
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	1.710
High resolution limit [Å]	1.650	1.650
Rmerge	0.039 *	0.239 *
Total number of observations	73479 *
Number of reflections	23688
Completeness [%]	88.8	78.8
Redundancy	3.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	9.5 *	293	sodium citrate, CHES, pH 9.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	reservoir	CHES	50 (mM)	pH9.5
3	1	reservoir	sodium citrate	0.5 (M)