1MDW

Crystal Structure of Calcium-Bound Protease Core of Calpain II Reveals the Basis for Intrinsic Inactivation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-09-07
Detector	MARRESEARCH
Wavelength(s)	1.54
Spacegroup name	P 1 21 1
Unit cell lengths	62.600, 80.600, 75.300
Unit cell angles	90.00, 103.90, 90.00

Refinement procedure

Resolution	50.000 * - 1.950
Rwork	0.207
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	1.191
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]	50.000 *	2.050
High resolution limit [Å]	1.950	1.950
Rmerge	0.049	0.356
Total number of observations	496583 *
Number of reflections	48591	4424 *
<I/σ(I)>	21.1	3.3
Completeness [%]	93.9	89.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	298	10% PEG6000, 0.1M Sodium Acetate, 30mM calcium chloride, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	10 (%(w/v))
2	1	reservoir	sodium acetate	0.1 (M)	pH5.5
3	1	reservoir		30 (mM)
4	1	drop	protein	15 (mg/ml)