1F48

CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-08-30
Detector	RIGAKU RAXIS IV
Spacegroup name	I 2 2 2
Unit cell lengths	73.523, 75.715, 222.714
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.370 - 2.300
R-factor	0.206
Rwork	0.206
R-free	0.26300
RMSD bond length	0.012
RMSD bond angle	1.800
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.086	0.651
Total number of observations	178456 *
Number of reflections	27783
<I/σ(I)>	18.8
Completeness [%]	98.2	91.4
Redundancy	6.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	303	Zhou, T., (1999) Acta Crystallogr., D55, 921. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	ADP	2 (mM)
3	1	drop		1 (mM)
4	1	drop		2 (mM)
5	1	drop		1 (mM)
6	1	drop	Bis-Tris propane	10 (mM)
7	1	reservoir	PEG3000	4 (%(w/v))