2BLG

STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 8.2

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1996-10
Detector	RIGAKU
Spacegroup name	P 32 2 1
Unit cell lengths	54.290, 54.290, 113.180
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 - 2.460
R-factor	0.232
Rwork	0.232
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	26.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.510
High resolution limit [Å]	2.460	2.460
Rmerge	0.080	0.390
Number of reflections	7203
<I/σ(I)>	10.5	2
Completeness [%]	97.1	89.6
Redundancy	2.34	2.34

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.2		pH 8.2

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25-30 (mg/ml)
2	1	reservoir	HEPES	0.01 (M)
3	1	reservoir	ammonium sulfate	2.2-2.8 (M)