2XQ0

Structure of yeast LTA4 hydrolase in complex with Bestatin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-3
Synchrotron site	MAX II
Beamline	I911-3
Temperature [K]	100
Detector technology	CCD
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	58.641, 99.874, 112.651
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.660 - 1.955
R-factor	0.1908
Rwork	0.190
R-free	0.24750
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2xpy
RMSD bond length	0.007
RMSD bond angle	1.112
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.700	2.000
High resolution limit [Å]	1.950	1.950
Rmerge	0.060	0.420
Number of reflections	46277
<I/σ(I)>	15.31	3.25
Completeness [%]	98.9	97.6
Redundancy	4	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1				15%GLYCEROL , 16.95% PEG 4000 , 8.5% ISOPROPANOL AND 0.1 M MMT BUFFER (PH 7.0) WITH 0.1 M BETAINE MONOHYDRATE AS AN ADDITIVE. THE RATIOS OF PROTEIN (9.6 MG/ML) WITH BESTATIN (6 MM), RESERVOIR AND ADDITIVE IN THE DROPS WERE 2:1:0.5.