1NBM

THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-05-12
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	281.000, 106.600, 138.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 3.000
R-factor	0.207
Rwork	0.207
R-free	0.29700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	ALUMINUM FLUORIDE INHIBITED FORM OF BOVINE MITOCHONDRIAL F1-ATPASE
RMSD bond length	0.005
RMSD bond angle	22.176 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	CCP4
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.160
High resolution limit [Å]	3.000	3.000
Rmerge	0.088	0.304
Number of reflections	70240
<I/σ(I)>	10.1	3.4
Completeness [%]	97.2	98
Redundancy	2.5	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	7.2 *	23 *	50MM TRIS-HCL, PH7.5, 200MM SODIUM CHLORIDE, 20MM MAGNESIUM SULPHATE, 1MM EDTA, 0.002% (W/V) PHENYL METHYLSULPHONYL FLUORIDE, 0.02%(W/V) SODIUM AZIDE, 10.5% (W/V) PEG MME 5000, 250UM AMP-PNP AND 5UM ADP.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	10 (mg/ml)
10	1	2	Tris-HCl	50 (mM)
11	1	2		200 (mM)
12	1	2	EDTA	1 (mM)
13	1	2	magnesium sulphate	20 (mM)
14	1	2	sodium azide	0.02 (%(w/v))
15	1	2	phenylmethylsulphonyl fluoride	0.002 (%(w/v))
2	1	1	Tris-HCl	100 (mM)
3	1	1		400 (mM)
4	1	1		4 (mM)
5	1	1	sodium azide	0.04 (%(w/v))
6	1	1	phenylmethylsulphonyl fluoride	0.004 (%(w/v))
7	1	1	PEG MME5000	12 (%(w/v))
8	1	1	AMP-PNP	2 (mM)
9	1	1	ADP	0.040 (mM)