1WQQ

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	1995-11-29
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	56.770, 61.070, 33.880
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
R-factor	0.164
Rwork	0.164
Structure solution method	DIFFERENCE MAP
Starting model (for MR)	WILD-TYPE OF HUMAN LYSOZYME
RMSD bond length	0.008
RMSD bond angle	23.800 *
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]	41.580	1.700
High resolution limit [Å]	1.587	1.587
Rmerge	0.038	0.125
Total number of observations	34462 *
Number of reflections	13271 *
<I/σ(I)>	16.6	3.79
Completeness [%]	80.1	69.2
Redundancy	2.6

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)