1WQN

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	1996-02-04
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	56.720, 61.050, 33.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
R-factor	0.165
Rwork	0.165
Structure solution method	DIFFERENCE MAP
Starting model (for MR)	WILD-TYPE OF HUMAN LYSOZYME
RMSD bond length	0.008
RMSD bond angle	24.300 *
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]	56.600	1.700
High resolution limit [Å]	1.584	1.584
Rmerge	0.061	0.171
Total number of observations	34844 *
Number of reflections	13928 *
<I/σ(I)>	13.1	3.15
Completeness [%]	84.7	68.9
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)