1LCY

Crystal Structure of the Mitochondrial Serine Protease HtrA2

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-07-01
Detector	FUJI
Wavelength(s)	1.1, 0.9788, 0.9791, 0.9638
Spacegroup name	H 3
Unit cell lengths	85.420, 85.420, 127.160
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 * - 2.000
R-factor	0.215 *
Rwork	0.235
R-free	0.24100 *
Structure solution method	MAD
RMSD bond length	0.005
RMSD bond angle	1.330
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MADSYS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.058 *	0.100 *
Number of reflections	23282
Completeness [%]	99.4 *	99.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.8	295	used macroseeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	citrate	100 (mM)	pH5.8
2	1	reservoir	lithium sulfate	1.0 (M)
3	1	reservoir		1.0 (M)