5HSA

Alcohol Oxidase AOX1 from Pichia Pastoris

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.1
Synchrotron site	BESSY
Beamline	14.1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2011-11-22
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.91842
Spacegroup name	P 1 21 1
Unit cell lengths	117.100, 165.190, 164.310
Unit cell angles	90.00, 95.67, 90.00

Refinement procedure

Resolution	40.877 - 2.350
R-factor	0.1787
Rwork	0.177
R-free	0.20490
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3q9t
RMSD bond length	0.006
RMSD bond angle	0.922
Data reduction software	XDS
Data scaling software	XSCALE (VERSION Oct 15, 2015 BUILT=20151231)
Phasing software	PHASER (2.5.0)
Refinement software	PHENIX (1.9.162)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.450
High resolution limit [Å]	2.350	50.000	2.350
Rmerge	0.107		0.782
Rmeas	0.128		0.965
Total number of observations	815776
Number of reflections	254643		29314
<I/σ(I)>	9.77		1.67
Completeness [%]	98.7		97.1
Redundancy	3.2		2.75
CC(1/2)	0.994		0.511

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	protein (15 mg/ml in 20 mM Na-HEPES, pH 7.5) was mixed with equal amount of reservoir solution containing 100 mM HEPES, pH 7.5, 200 mM CaCl2 and 33.3 % (w/v) PEG 400.