130L

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, 96.800
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 * - 1.700
R-factor	0.164
RMSD bond length	0.018
RMSD bond angle	2.600
Refinement software	TNT

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000 *
High resolution limit [Å]	1.700 *
Rmerge	0.122 *
Number of reflections	20832 *

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)