2GM3

Crystal Structure of an Universal Stress Protein Family Protein from Arabidopsis Thaliana At3g01520 with AMP Bound

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2005-06-13
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97934
Spacegroup name	P 1
Unit cell lengths	63.351, 65.662, 73.014
Unit cell angles	75.45, 75.04, 66.11

Refinement procedure

Resolution	40.700 - 2.461
R-factor	0.22065
Rwork	0.218
R-free	0.26070
Structure solution method	SAD
RMSD bond length	0.016
RMSD bond angle	1.501
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	RESOLVE (2.06)
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.700	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.058	0.239
Number of reflections	36006
<I/σ(I)>	9.913	4.406
Completeness [%]	97.2	89.4
Redundancy	3.7	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, 0.005 MES PH 7.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (18% PEG 2K, 5% DMSO, 0.10 M PIPES PH 6.5) Crystals cryo-protected with 20% PEG 2K, 0.1 M TRIS PH 8, and a final concentration of 20 % Ethylene glycol, temperature 293K, VAPOR DIFFUSION, HANGING DROP
1	VAPOR DIFFUSION, HANGING DROP		293	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, 0.005 MES PH 7.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (18% PEG 2K, 5% DMSO, 0.10 M PIPES PH 6.5) Crystals cryo-protected with 20% PEG 2K, 0.1 M TRIS PH 8, and a final concentration of 20 % Ethylene glycol, temperature 293K, VAPOR DIFFUSION, HANGING DROP