3B7S

[E296Q]LTA4H in complex with RSR 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	2004-04-24
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97
Spacegroup name	P 21 21 21
Unit cell lengths	78.508, 87.351, 99.769
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.465
R-factor	0.128
Rwork	0.128
R-free	0.16900
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1h19
RMSD bond length	0.015
RMSD bond angle	0.034
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	SHELX

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	18.254	1.540
High resolution limit [Å]	1.465	1.465
Rmerge	0.059	0.261
Total number of observations		58235
Number of reflections	116485
<I/σ(I)>	7.8	2.7
Completeness [%]	98.2	88.4
Redundancy	4.3	3.8

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