1IOC

CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-18B
Synchrotron site	Photon Factory
Beamline	BL-18B
Temperature [K]	100
Detector technology	DIFFRACTOMETER
Collection date	1999-11-27
Detector	WEISSENBERG
Wavelength(s)	1
Spacegroup name	P 61 2 2
Unit cell lengths	90.120, 90.120, 92.640
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.400
R-factor	0.21
Rwork	0.210
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	EAEA human lysozyme
Data reduction software	DENZO
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
High resolution limit [Å]	2.400
Rmerge	0.118
Total number of observations	72930 *
Number of reflections	9168
Completeness [%]	99.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	10 *	Goda, S., (2000) Protein Eng., 13, 299. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	cadmium chloride	0.1 (M)
3	1	reservoir	sodium acetate	0.1 (M)
4	1	reservoir	PEG400	30 (%(v/v))