1IRU

Crystal Structure of the mammalian 20S proteasome at 2.75 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL41XU
Synchrotron site	SPring-8
Beamline	BL41XU
Temperature [K]	100
Detector technology	CCD
Detector	MARRESEARCH
Wavelength(s)	1.00
Spacegroup name	P 21 21 21
Unit cell lengths	316.700, 205.900, 116.000
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	65.000 - 2.750
R-factor	0.25 *
Rwork	0.250
R-free	0.29400
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	X-PLOR
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000 *	2.820
High resolution limit [Å]	2.750	2.750
Rmerge	0.095 *	0.406 *
Total number of observations	733250 *
Number of reflections	189429
Completeness [%]	96.3	70

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	25 *	Tomisugi, Y., (2000) J. Biochem., 127, 941. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	magnesium acetate	0.15 (M)
2	1	reservoir	sodium cacodylate	0.1 (M)	pH6.5
3	1	reservoir	MPD	35 (%)