1QZ5

Structure of rabbit actin in complex with kabiramide C

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Temperature [K]	100
Detector technology	CCD
Collection date	2002-08-23
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9
Spacegroup name	P 21 21 21
Unit cell lengths	69.919, 70.617, 75.130
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.450
R-factor	0.17001
Rwork	0.169
R-free	0.18800 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.670 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	1.500
High resolution limit [Å]	1.450	1.450
Rmerge	0.044	0.123
Total number of observations	542898 *
Number of reflections	65708
<I/σ(I)>	47.1	13.9
Completeness [%]	98.5	95.7 *
Redundancy	8.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Batch method *	5.5	293	Crystals of the actin-kabiramide C complex were grown by small-scale batch by mixing equal volumes of the complex and 100 mM MES, 18% (w/v) polyethylene glycol 1500, 12% (w/v) 1,6-hexanediol, 100 mM CaCl2, 1 mM sodium azide, 1 mM TCEP, pH 5.5, Batch, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	10-12 (mg/ml)
2	1	1	MES	100 (mM)	pH5.5
3	1	1	PEG1500	18 (%(w/v))
4	1	1	1,6-hexanediol	12 (%(w/v))
5	1	1		100 (mM)
6	1	1		1 (mM)
7	1	1	TCEP	1 (mM)