1V1G

Structure of the Arabidopsis thaliana SOS3 complexed with Calcium(II) ion

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM16
Synchrotron site	ESRF
Beamline	BM16
Temperature [K]	100
Collection date	2003-10-15
Spacegroup name	I 41
Unit cell lengths	91.600, 91.600, 85.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.700
R-factor	0.237
Rwork	0.235
R-free	0.26400
Structure solution method	SAD
RMSD bond length	0.014
RMSD bond angle	1.735
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SHARP
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	62.000	2.850
High resolution limit [Å]	2.700	2.700
Rmerge	0.057	0.540
Number of reflections	9757
<I/σ(I)>	4.4	1.4
Completeness [%]	100.0	99.6
Redundancy	3.7	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	4.8		PRIOR TO CRYSTALLIZATION THE PROTEIN WAS PREINCUBATED WITH 3.8 MM CACL2 TO REACH A FINAL PROTEIN CONCENTRATION OF 10 MG/ML AND A PRTEIN:METAL ION RATIO 1:10. CRYSTALLIZATION EXPERIMENTS WERE CARRIED OUT AT ROOM TEMPERATURE. CRYSTALS WERE GROWN USING VAPOUR DIFFUSION TECHNIQUES FROM DROPS CONTAINING SOS3-CA, RESERVOIR SOLUTIONS (24%(W/V) METHYL-PENTANEDIOL, 18%(W/V) POLYETHYLENE GLYCOL 4000 AND 0.1 NA-CITRATE PH 4.8) AND NAI 1M IN A RATIO 2:1:0.75