1O06

Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-01-10
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 62 2 2
Unit cell lengths	34.967, 34.967, 64.243
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 * - 1.450
R-factor	0.18884
Rwork	0.185
R-free	0.22300 *
Structure solution method	SAD
RMSD bond length	0.008
RMSD bond angle	1.365
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.500
High resolution limit [Å]	1.450	1.450
Rmerge	0.034	0.135
Total number of observations	32073 *
Number of reflections	4525
<I/σ(I)>	33.5	10.5
Completeness [%]	99.3	94.2
Redundancy	7.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5 *	23 *	0.08M sodium cacodylate, 0.16M zinc acetate, 10.4% PEG-8000, 20% glycerol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K
1	VAPOR DIFFUSION, SITTING DROP	7.5 *	23 *	0.08M sodium cacodylate, 0.16M zinc acetate, 10.4% PEG-8000, 20% glycerol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Vps27p-2	1.6 (mM)
2	1	drop	selenomethionine-substituted ubiquitin	0.8 (mM)
3	1	drop	Tris	50 (mM)	pH7.5
4	1	drop		150 (mM)
5	1	reservoir	sodium cacodylate	0.08 (M)	pH6.5
6	1	reservoir	zinc acetate	0.16 (M)
7	1	reservoir	PEG8000	10.4 (%)
8	1	reservoir	glycerol	20 (%)