4QT6

Crystal structure of the SPRY domain of human HERC1

Experimental procedure

Experimental method	SAD
Source type	ROTATING ANODE
Source details	RIGAKU FR-E SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2014-06-26
Detector	RIGAKU SATURN A200
Wavelength(s)	1.5406
Spacegroup name	I 2 3
Unit cell lengths	99.730, 99.730, 99.730
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.640
R-factor	0.1711
Rwork	0.170
R-free	0.21230
Structure solution method	SAD
RMSD bond length	0.009
RMSD bond angle	1.433
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	SOLVE (2 .13)
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.670
High resolution limit [Å]	1.640	4.450	1.640
Rmerge	0.056	0.029	0.864
Number of reflections	20404
<I/σ(I)>	80.4
Completeness [%]	99.9	98.6	100
Redundancy	27.8	25.6	27.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.5 uL protein (mixed 1:700 w/w chymotrypsin:protein before setup) + 0.5 uL well solution (16% w/v PEG 8000, 0.04 M potassium phosphate monobasic, 20% v/v glycerol) + 0.1 uL 40% formamide (4% final concentration), VAPOR DIFFUSION, SITTING DROP, temperature 293K