1N9E

Crystal structure of Pichia pastoris Lysyl Oxidase PPLO

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-1
Synchrotron site	SSRL
Beamline	BL9-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-12-17
Detector	MAR scanner 345 mm plate
Spacegroup name	C 1 2 1
Unit cell lengths	248.442, 121.125, 151.841
Unit cell angles	90.00, 124.64, 90.00

Refinement procedure

Resolution	24.600 - 1.650
R-factor	0.16029
Rwork	0.161
R-free	0.18700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1oac
RMSD bond length	0.010
RMSD bond angle	1.500 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.600	1.690
High resolution limit [Å]	1.650	1.650
Rmerge	0.060 *	0.420
Number of reflections	419014	28231 *
<I/σ(I)>	9.1	2.2
Completeness [%]	94.7	90.7 *
Redundancy	2.8	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7	277 *	Lee, M., (2002) Acta Cryst., D58, 2177. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	reservoir	PEG4000	25 (%)
3	1	reservoir	ammonium sulfate	175 (mM)