2HEB

CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

Experimental procedure

Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-6B
Synchrotron site	Photon Factory
Beamline	BL-6B
Detector technology	IMAGE PLATE
Collection date	1996-12-07
Spacegroup name	P 21 21 21
Unit cell lengths	56.800, 61.220, 33.760
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.200
R-factor	0.124
Rwork	0.124
RMSD bond length	0.008
RMSD bond angle	1.520
Data reduction software	DENZO
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
High resolution limit [Å]	2.000 *
Rmerge	0.071	0.185 *
Total number of observations	21591 *
Number of reflections	5702
Completeness [%]	67.7	56.2 *
Redundancy	3.87

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.5 *	10 *	Takano, K., (1997) Biochemistry, 36, 688. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir		2.5 (M)
3	1	reservoir	acetate	20 (mM)