2MEG

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

Experimental procedure

Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-18B
Synchrotron site	Photon Factory
Beamline	BL-18B
Temperature [K]	283
Detector technology	IMAGE PLATE
Collection date	1996-12-12
Spacegroup name	P 21 21 21
Unit cell lengths	57.100, 61.060, 33.760
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
R-factor	0.151
Rwork	0.151
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	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]		1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.052	0.180
Total number of observations	42094 *
Number of reflections	10582 *
<I/σ(I)>		8.8
Completeness [%]	92.2	80.9
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)