1SPP

THE CRYSTAL STRUCTURES OF TWO MEMBERS OF THE SPERMADHESIN FAMILY REVEAL THE FOLDING OF THE CUB DOMAIN

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	285
Detector technology	IMAGE PLATE
Collection date	1995-11
Detector	MARRESEARCH
Spacegroup name	P 32 2 1
Unit cell lengths	96.370, 96.370, 71.320
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.400
R-factor	0.2
Rwork	0.200
R-free	0.25900
Structure solution method	MIR
RMSD bond length	0.009
RMSD bond angle	28.390 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((ROTAVATA))
Phasing software	CCP4
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.940	2.500
High resolution limit [Å]	2.400	2.400
Rmerge	0.057	0.265 *
Total number of observations	61270 *
Number of reflections	14809
<I/σ(I)>	7.1	3
Completeness [%]	97.0	98.4
Redundancy	4.1	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7 *	22 *	PROTEIN WAS CRYSTALLIZED FROM 30% (W/V) PEG 2000, 100 MM AMMONIUM ACETATE, PH 6.5. THE INITIAL PROTEIN CONCENTRATION WAS 15 MG/ML

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	sodium phosphate	50 (mM)
3	1	reservoir	PEG2000	30 (%(w/v))
4	1	reservoir	ammonium acetate	0.1 (M)