1B5Z

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	283
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	64.670, 110.300, 43.640
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.200
R-factor	0.19 *
Rwork	0.148
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	I56F MUTANT HUMAN LYSOZYME
RMSD bond length	0.009
RMSD bond angle	1.480
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]	100.000	1.900
High resolution limit [Å]	1.810	1.810
Rmerge	0.051
Total number of observations	68449 *
Number of reflections	23175
<I/σ(I)>		2.4
Completeness [%]	79.4	52.6
Redundancy	3

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)