1HF4

STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME CRYSTALS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-01-15
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	27.940, 62.730, 60.250
Unit cell angles	90.00, 90.76, 90.00

Refinement procedure

Resolution	6.000 - 1.450
R-factor	0.215
Rwork	0.215
R-free	0.25600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5lym
RMSD bond length	0.006
RMSD bond angle	23.800 *
Data reduction software	MOSFLM
Data scaling software	Agrovata
Phasing software	X-PLOR (3.853)
Refinement software	X-PLOR (3.853)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000	1.490
High resolution limit [Å]	1.450	1.450
Rmerge	0.123 *	0.160
Number of reflections	35206
<I/σ(I)>	3.1	4.5
Completeness [%]	95.5	87
Redundancy	7.7	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	5 *	293	CRYSTALS OF NITRATE-LYSOZYME WERE GROWN UNDER A MICRO GRAVITY ENVIRONMENT DURING THE USML-2 MISSION LAUNCHED ON OCTOBER 1995 (SHUTTLE COLUMBIA). THE CRYSTALLIZATION SETUP WAS THE APCF DEVELOPPED BY EUROPEAN SPACE AGENCY. PROTEIN CONCENTRATION 10 MG/ML IN 50 MM SODIUM ACETATE BUFFER AT PH 4.5. GRADIENT CONCENTRATION APPLIED FROM 0 TO FINAL 290 MM AT 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	10 (mg/ml)
2	1	1	sodium acetate	50 (mM)
3	1	2	sodium nitrate	0-290 (mM)