2MEA

CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	283
Detector technology	IMAGE PLATE
Collection date	1997-04-18
Detector	RIGAKU
Spacegroup name	P 21 21 21
Unit cell lengths	64.740, 110.550, 43.510
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.200
R-factor	0.172
Rwork	0.172
Structure solution method	ISOMORPHOUS METHOD
Starting model (for MR)	WILD-TYPE OF HUMAN LYSOZYME
RMSD bond length	0.008
RMSD bond angle	23.900 *
Data reduction software	PROCESS
Data scaling software	PROCESS
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]		2.500
High resolution limit [Å]	2.060	1.800 *
Rmerge	0.052	0.118
Total number of observations	46922 *
Number of reflections	16889 *
<I/σ(I)>		4.2
Completeness [%]	84.2	74.6
Redundancy	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.5	10 *	Takano, K., (1995) J.Mol.Biol., 254, 62. *

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)