1OUA

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	283
Detector technology	IMAGE PLATE
Collection date	1996-04-23
Detector	RIGAKU
Spacegroup name	P 21 21 21
Unit cell lengths	56.690, 61.030, 33.790
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
R-factor	0.148
Rwork	0.148
Structure solution method	DIFFERENCE FOURIER
RMSD bond length	0.009
RMSD bond angle	24.159 *
Data reduction software	RIGAKU (SOFTWARE)
Data scaling software	RIGAKU
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
High resolution limit [Å]	1.800
Rmerge	0.056
Total number of observations	28187 *
Number of reflections	9220
Completeness [%]	80.4
Redundancy	3.05

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.5	10 *	pH 4.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir		2.2 (M)
2	1	reservoir	acetate	20 (mM)
3	1	drop	protein	5.6 (mg/ml)