1XMB

X-ray structure of IAA-aminoacid hydrolase from Arabidopsis thaliana gene AT5G56660

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	110
Detector technology	CCD
Collection date	2004-08-01
Detector	APS-1
Wavelength(s)	0.96411
Spacegroup name	P 32 2 1
Unit cell lengths	75.264, 75.264, 130.880
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	24.210 - 2.000
R-factor	0.159
Rwork	0.157
R-free	0.20390
Structure solution method	SAD
RMSD bond length	0.018
RMSD bond angle	1.587
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE (2.06)
Refinement software	REFMAC (refmac_5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	24.210	50.000	2.070
High resolution limit [Å]	2.000	4.310	2.000
Rmerge	0.043	0.024	0.334
Total number of observations		3132	2939
Number of reflections	29672
<I/σ(I)>	22		3.8
Completeness [%]	99.9	98.8	99.9
Redundancy	8.4		6.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	9	293	10 mg/mL PROTEIN, 0.080 M MAGNESIUM SULFATE, 14 % PEG 1500, 0.100 M CHES, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	9	293	10 mg/mL PROTEIN, 0.080 M MAGNESIUM SULFATE, 14 % PEG 1500, 0.100 M CHES, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K