2MEB

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	1996-12-27
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	56.750, 61.020, 33.870
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
R-factor	0.156
Rwork	0.156
Structure solution method	ISOMORPHOUS METHOD
Starting model (for MR)	WILD-TYPE OF HUMAN LYSOZYME
RMSD bond length	0.008
RMSD bond angle	24.000 *
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]		1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.036	0.086
Total number of observations	36209 *
Number of reflections	10512 *
<I/σ(I)>		8.4
Completeness [%]	91.8	85.8
Redundancy	2.5

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)