1ZXU

X-ray structure of protein from arabidopsis thaliana AT5G01750

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Temperature [K]	100
Detector technology	CCD
Collection date	2005-05-25
Detector	ADSC
Wavelength(s)	0.97900, 0.96110
Spacegroup name	P 21 21 21
Unit cell lengths	41.066, 57.499, 75.359
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.690 - 1.700
R-factor	0.191
Rwork	0.189
R-free	0.23100
Structure solution method	MAD
RMSD bond length	0.020
RMSD bond angle	1.723
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (refmac_5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.760
High resolution limit [Å]	1.700	3.660	1.700
Rmerge	0.080	0.058	0.454
Number of reflections	20314
<I/σ(I)>	18.016		4.422
Completeness [%]	100.0		99.9
Redundancy	13.6	12.9	11.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	BATCH SEEDING	5.5	293	10 MG/ML PROTEIN, 25% PEG 3350, 0.2 M AMMONIUM ACETATE, 0.1 M BISTRIS, temperature 293K, pH 5.5, BATCH SEEDING
1	BATCH SEEDING	5.5	293	10 MG/ML PROTEIN, 25% PEG 3350, 0.2 M AMMONIUM ACETATE, 0.1 M BISTRIS, temperature 293K, pH 5.5, BATCH SEEDING