1AOL

FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-10
Detector	RIGAKU RAXIS
Spacegroup name	P 21 21 21
Unit cell lengths	55.300, 68.400, 80.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.223
Rwork	0.223
R-free	0.26400
Structure solution method	MIR
RMSD bond length	0.014
RMSD bond angle	2.900
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.067 *
Number of reflections	20321
<I/σ(I)>	11	6
Completeness [%]	97.2	93.9
Redundancy	2.5	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5	20 *	PROTEIN WAS CRYSTALLIZED FROM 150 MM ZINC ACETATE, 100 MM SODIUM CACODYLATE, PH 6.5, 19% PEG 8000

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	calcium acetate	150 (mM)
2	1	reservoir	sodium cacodylate	100 (mM)
3	1	reservoir	PEG8000	19 (%)