1BOU

THREE-DIMENSIONAL STRUCTURE OF LIGAB

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	300
Detector technology	IMAGE PLATE
Collection date	1998-03-09
Detector	RIGAKU
Spacegroup name	P 1 21 1
Unit cell lengths	65.400, 66.500, 119.800
Unit cell angles	90.00, 92.50, 90.00

Refinement procedure

Resolution	60.000 - 2.200
R-factor	0.16 *
Rwork	0.149
R-free	0.21600 *
Structure solution method	MIRAS
RMSD bond length	0.016 *
RMSD bond angle	2.100 *
Data reduction software	PROCESS
Data scaling software	PROCESS
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.000	2.250
High resolution limit [Å]	2.200	2.200
Rmerge	0.047	0.139
Total number of observations	80490 *
Number of reflections	43335
<I/σ(I)>	9.8	2.9
Completeness [%]	86.5	58
Redundancy	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	20 *	Sugimoto, K., (1999) Protein Peptide Lett., 6, 55. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	37.0 (mg/ml)
2	1	drop	Tris-HCl	100 (mM)
3	1	reservoir	ammonium sulfate	50 (%sat)
4	1	reservoir	Tris-HCl	100 (mM)