129L

STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT

Experimental procedure

Spacegroup name	P 32 2 1
Unit cell lengths	61.000, 61.000, 97.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 * - 1.700
R-factor	0.165
RMSD bond length	0.017
RMSD bond angle	2.700
Refinement software	TNT

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000 *
High resolution limit [Å]	1.700 *
Rmerge	0.048 *
Number of reflections	17845 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *		5 *	used to seeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	7.5-10 (mg/ml)
2	1	1	sodium potassium phosphate	1.05 (M)
3	1	1		0.275 (M)
4	1	1		0.01 (%)
5	1	1		0.2 (%)
6	1	2	sodium potassium phosphate	2 (M)