3RRW

Crystal structure of the TL29 protein from Arabidopsis thaliana

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-3
Synchrotron site	MAX II
Beamline	I911-3
Temperature [K]	100
Detector technology	CCD
Collection date	2009-05-06
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97926
Spacegroup name	P 41 21 2
Unit cell lengths	92.350, 92.350, 143.460
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.170 - 2.500
R-factor	0.22753
Rwork	0.225
R-free	0.27550
Structure solution method	SAD
RMSD bond length	0.015
RMSD bond angle	1.336
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHENIX
Refinement software	REFMAC (5.5.0072)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.280	2.640
High resolution limit [Å]	2.500	2.500
Rmerge	0.092	0.346
Number of reflections	22173
<I/σ(I)>		4.3
Completeness [%]	99.9	100
Redundancy	7.2	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.8	291	Reservoir solution: 16 % PEG 4000, 0.2M potassium phosphate, 10 % glycerol. Protein solution: 16 mM sodium phosphate, 0.1 M NaCl, 10 % glycerol, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K