1MOL

TWO CRYSTAL STRUCTURES OF A POTENTLY SWEET PROTEIN: NATURAL MONELLIN AT 2.75 ANGSTROMS RESOLUTION AND SINGLE-CHAIN MONELLIN AT 1.7 ANGSTROMS RESOLUTION

Experimental procedure

Spacegroup name	P 1 21 1
Unit cell lengths	46.360, 49.090, 40.720
Unit cell angles	90.00, 102.86, 90.00

Refinement procedure

Resolution	6.000 - 1.700
R-factor	0.174
Rwork	0.174
RMSD bond length	0.015
RMSD bond angle	2.860
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
High resolution limit [Å]	1.600 *
Rmerge	0.064 *
Total number of observations	59663 *
Number of reflections	19162 *
Completeness [%]	82.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.2 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	drop	sodium phosphate	10 (mM)
3	1	drop	PEG8000	4 (%(w/v))
4	1	reservoir	PEG8000	33 (%(w/v))