1E32

Structure of the N-Terminal domain and the D1 AAA domain of membrane fusion ATPase p97

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-09-15
Detector	MARRESEARCH
Spacegroup name	P 6 2 2
Unit cell lengths	146.000, 146.000, 84.700
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 - 2.900
R-factor	0.224
Rwork	0.224
R-free	0.28300
Structure solution method	MIRAS
RMSD bond length	0.007
RMSD bond angle	1.530
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.000
High resolution limit [Å]	2.900	2.900
Rmerge	0.090	0.300
Number of reflections	12114
<I/σ(I)>	9.7
Completeness [%]	99.8	100
Redundancy	19.3 *	15

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6		3.8-4.2 M NAFORMATE, 10% GLYCEROL, 5% PEG600, PH 5.5-6.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	16 (mg/ml)
2	1	reservoir	sodium formate	3.8-4.2 (M)
3	1	reservoir	glycerol	10 (%)
4	1	reservoir	PEG600	5 (%)