4W79

Crystal Structure of Human Protein N-terminal Glutamine Amidohydrolase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Detector technology	CCD
Collection date	2008-02-06
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97942
Spacegroup name	P 21 21 21
Unit cell lengths	34.322, 64.039, 113.660
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	56.830 - 1.500
R-factor	0.145
Rwork	0.144
R-free	0.16990
RMSD bond length	0.017
RMSD bond angle	1.913
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	100.000	100.000	1.530
High resolution limit [Å]	1.500	3.700	1.500
Rmerge	0.105	0.058	0.543
Total number of observations	498430
Number of reflections	40943
<I/σ(I)>	8.9
Completeness [%]	99.5	99.5	95.9
Redundancy	12.2	12.6	6.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	291	PROTEIN SOLUTION (10 MG/ML SE-MET PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, BIS-TRIS PH 7.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (1% ETHYLENE GLYCOL, 1.8 M AMMONIUM SULFATE, 0.10 M MES PH 6.0). CRYOPROTECTED IN FOUR STAGES WITH WELL SOLUTION USING 0 TO 25 % ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K