1G65

Crystal structure of epoxomicin:20s proteasome reveals a molecular basis for selectivity of alpha,beta-epoxyketone proteasome inhibitors

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	90
Detector technology	IMAGE PLATE
Collection date	1999-04-19
Detector	MARRESEARCH
Wavelength(s)	1.1
Spacegroup name	P 1 21 1
Unit cell lengths	135.200, 300.200, 144.020
Unit cell angles	90.00, 112.98, 90.00

Refinement procedure

Resolution	20.000 - 2.250
R-factor	0.283 *
Rwork	0.283
R-free	0.33600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	wt yeast 20S proteasome (1RYP)
RMSD bond length	0.012 *
RMSD bond angle	1.946 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.340
High resolution limit [Å]	2.250	2.250
Rmerge	0.113	0.395
Total number of observations	1336712 *
Number of reflections	427960
<I/σ(I)>	8.3
Completeness [%]	91.6	91.1
Redundancy	2.6	1.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	24 *	0.1M Mes, pH 6.8 11% MPD 25mM MgAc2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	40 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)	pH7.5
3	1	drop	EDTA	1 (mM)
4	1	reservoir	magnesium acetate	30 (mM)
5	1	reservoir	MES	100 (mM)	pH6.9
6	1	reservoir	MPD	11 (%)