1O0E

1.9 Angstrom Crystal Structure of a plant cysteine protease Ervatamin C

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200B
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1999-01-04
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	43.729, 82.691, 133.048
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 * - 1.900
R-factor	0.177
Rwork	0.177
R-free	0.19000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1iwd
RMSD bond length	0.006
RMSD bond angle	24.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.940
High resolution limit [Å]	1.900	1.900
Rmerge	0.060	0.560
Total number of observations	157915 *
Number of reflections	38978
<I/σ(I)>	20.15	2.86
Completeness [%]	97.9	99.8
Redundancy	4.05

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	PEG8000, potassium phosphate monobasic, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	13 (mg/ml)
2	1	drop	sodium phosphate	0.01 (M)	pH7.0
3	1	reservoir	potassium dihydrogen orhtophosphate	0.05 (M)
4	1	reservoir	PEG8000	20 (%(w/v))