1A29

CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:2 COMPLEX)

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-02
Detector	RIGAKU
Spacegroup name	P 32 2 1
Unit cell lengths	40.750, 40.750, 177.570
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	59.190 - 2.740
R-factor	0.1971
Rwork	0.197
R-free	0.26540 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1lin
RMSD bond length	0.006
RMSD bond angle	21.500 *
Data reduction software	bioteX
Data scaling software	bioteX
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	87.700	2.860
High resolution limit [Å]	2.740	2.740
Rmerge	0.074 *	0.092
Total number of observations	12467 *
Number of reflections	5036 *
<I/σ(I)>	11.3	1.84
Completeness [%]	95.1 *	98.2
Redundancy	1.92	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.2 *	6-10 *	PROTEIN WAS CRYSTALLIZED BY SITTING DROP TECHNIQUE IN THE COLD ROOM (8 DEGREES C +/- 2 DEGREES C) BY MIXING 4 MICROLITERS OF 1 MM PROTEIN CONTAINING 1.2-1.5 MM TFP IN 5 MM CACL2 WITH 4 MICROLITERS OF THE RESERVOIR SOLUTION (1 ML 10 MM SODIUM CACODYLATE/HCL BUFFER, PH 5.2-5.6 WITH 10 MM CACL2, 25-30 % (W/V) POLYETHYLENE GLYCOL 6000), CRYSTAL GROWTH TOOK 2-3 WEEKS., pH 5.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	1 (mM)
2	1	drop	trifluoperazine	1.2-1.7 (mM)
3	1	drop		5 (mM)
4	1	reservoir	sodium cacodylate-HCl	10 (mM)
5	1	reservoir		10 (mM)
6	1	reservoir	PEG6000	30 (%(w/v))