32C2

STRUCTURE OF AN ACTIVITY SUPPRESSING FAB FRAGMENT TO CYTOCHROME P450 AROMATASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	287
Detector technology	IMAGE PLATE
Detector	RIGAKU
Spacegroup name	P 21 21 21
Unit cell lengths	154.890, 73.510, 36.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	99.000 - 3.000
R-factor	0.2124 *
Rwork	0.213
R-free	0.31700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1flr
RMSD bond length	1.052
RMSD bond angle	26.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	CNS (0.4)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000	3.190
High resolution limit [Å]	2.900	3.000
Rmerge	0.091 *
Total number of observations	42185 *
Number of reflections	9161
Completeness [%]	91.1	71.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.4		0.2M SODIUM ACETATE, PH 4.4 @ 12 MG/ML. PRECIPITANT WAS 25% PEG 3350, pH 4.40

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	sodium acetate	0.2 (M)
2	1	drop	sodium azide	10 (mM)
3	1	drop	Fab	12 (mg/ml)
4	1	reservoir	PEG3350	25 (%)
5	1	reservoir	sodium acetate	0.2 (M)
6	1	reservoir		10 (mM)