1WQO

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	283
Detector technology	IMAGE PLATE
Collection date	1996-04-21
Detector	RIGAKU
Spacegroup name	P 21 21 21
Unit cell lengths	56.650, 61.020, 33.740
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
R-factor	0.17
Rwork	0.170
Structure solution method	DIFFERENCE MAP
Starting model (for MR)	WILD-TYPE OF HUMAN LYSOZYME
RMSD bond length	0.009
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]	61.000	1.700
High resolution limit [Å]	1.586	1.586
Rmerge	0.065	0.148
Total number of observations	48488 *
Number of reflections	15639 *
<I/σ(I)>	14.7	4.51
Completeness [%]	94.8	87
Redundancy	3.1

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)