1B5V

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-6A
Synchrotron site	Photon Factory
Beamline	BL-6A
Temperature [K]	283
Detector technology	DIFFRACTOMETER
Collection date	1997-11-27
Detector	WEISSENBERG
Spacegroup name	P 21 21 21
Unit cell lengths	56.690, 60.790, 33.680
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.170
R-factor	0.161
Rwork	0.161
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	WILD-TYPE OF HUMAN LYSOZYME
RMSD bond length	0.009
RMSD bond angle	1.600
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.250
High resolution limit [Å]	2.170	2.170
Rmerge	0.070	0.118
Total number of observations	17842 *
Number of reflections	5960
<I/σ(I)>	17	9.7
Completeness [%]	92.2	87.9
Redundancy	3	2.7

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)