3B7T

[E296Q]LTA4H in complex with Arg-Ala-Arg substrate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	CCD
Collection date	2005-10-05
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97
Spacegroup name	P 21 21 21
Unit cell lengths	78.490, 87.785, 99.916
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.300
Rwork	0.206
R-free	0.27300
Starting model (for MR)	1h19
RMSD bond length	0.007
RMSD bond angle	1.300
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.420	2.500
High resolution limit [Å]	2.300	2.300
Rmerge	0.125	0.801
Number of reflections	57220	12804
<I/σ(I)>	7.45	2.8
Completeness [%]	96.6	97.7
Redundancy		2.54

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	liquid-liquid diffusion		298	TRI-PEPTIDE WAS CO-CRYSTALLIZED WITH [E296Q]LTA4H BY LIQUID-LIQUID DIFFUSION IN MELTING-POINT CAPILLARIES. A TRIS-BUFFERED (10 mM, PH 7.5) SOLUTION OF PROTEIN AND TRIPEPTIDE, MOLAR RATIO 1:10 (~70 MICROM PROTEIN), WAS LAYERED ON THE PRECIPITATE SOLUTION CONTAINING 28% (WEIGHT/VOLUME) POLYETHYLENE GLYCOL (MW 8000), 50 mM NA ACETATE, 100 mM IMIDAZOLE, PH 6.8, AND 5 MM YBCL3. CRYSTALS WERE ADDITIONALLY SOAKED IN SOLUTIONS WITH INCREASED TRI-PEPTIDE CONCENTRATION PRIOR TO DATA COLLECTION, liquid-liquid diffusion, temperature 298K