1BP1

CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	300
Detector technology	IMAGE PLATE
Collection date	1994-02
Detector	RIGAKU
Spacegroup name	C 1 2 1
Unit cell lengths	185.600, 33.000, 85.200
Unit cell angles	90.00, 101.60, 90.00

Refinement procedure

Resolution	50.000 - 2.400
R-factor	0.225
Rwork	0.225
R-free	0.29500
Structure solution method	MIRAS
RMSD bond length	0.007
RMSD bond angle	26.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.500
High resolution limit [Å]	2.400	2.400
Rmerge	0.072 *
Number of reflections	18908
<I/σ(I)>		2.6
Completeness [%]	92.7	94.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.8		CRYSTALLIZED IN 12% PEG 8000, 0.2 M MG ACETATE, 0.1 NA CACODYLATE PH 6.8

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8.5 (mg/ml)
2	1	reservoir	PEG8000	12 (%(w/v))
3	1	reservoir	magnesium acetate	200 (mM)
4	1	reservoir	sodium cacodylate	100 (mM)