1BEA

BIFUNCTIONAL HAGEMAN FACTOR/AMYLASE INHIBITOR FROM MAIZE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1995-05
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 42 21 2
Unit cell lengths	57.120, 57.120, 80.240
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.000 - 1.950
R-factor	0.195
Rwork	0.195
R-free	0.28700
Structure solution method	MIR/MOLECULAR REPLACEMENT
Starting model (for MR)	1bip
RMSD bond length	0.016
RMSD bond angle	25.200 *
Data reduction software	PROCESS
Data scaling software	PROCESS
Phasing software	EPMR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.000	1.970
High resolution limit [Å]	1.950	1.940
Number of reflections	9031
Completeness [%]	92.0	65.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.5		PROTEIN WAS CRYSTALLIZED FROM 30% PEG-400, 100 MM HEPES PH 7.5, 0.2 M MGCL2. CRYSTAL WAS SOAKED IN 0.1 M SODIUM ACETATE, 30% PEG-400, 0.2 M MGCL2, PH 5.8 PRIOR TO DATA COLLECTION.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25 (mg/ml)
2	1	reservoir	PEG400	30 (%)
3	1	reservoir		0.2 (M)
4	1	reservoir	HEPES	0.1 (M)	pH7.5