1OUE

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	283
Detector technology	IMAGE PLATE
Collection date	1995-07-26
Detector	RIGAKU
Spacegroup name	P 21 21 21
Unit cell lengths	56.700, 61.120, 33.760
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
R-factor	0.158
Rwork	0.158
RMSD bond length	0.008
RMSD bond angle	23.975 *
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	0.046
Total number of observations	36385 *
Number of reflections	10428
Completeness [%]	91.3
Redundancy	3.48

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)