1ILZ

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 6.1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	120
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Wavelength(s)	1.00
Spacegroup name	P 31 2 1
Unit cell lengths	78.168, 78.168, 101.685
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	31.000 - 2.500
R-factor	0.222 *
Rwork	0.222
R-free	0.26800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Starting model 1QD5 with the active site residues truncated to ala and all waters and detergent molecules removed. All remaining atoms have been given a random shift of almost 0.5 Angstrom in all directions.
RMSD bond length	0.006
RMSD bond angle	1.136
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.000	2.540
High resolution limit [Å]	2.500	2.500
Rmerge	0.037	0.113
Total number of observations	150605 *
Number of reflections	12728 *	611 *
<I/σ(I)>	39.2	8.3
Completeness [%]	98.8	96.1
Redundancy	11.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.6 *	293	MPD, calcium chloride, bis-tris buffer, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	MPD	27 (%(v/v))
2	1	reservoir		0.4-1.0 (mM)
3	1	reservoir	Bis-Tris	0.1 (M)
4	1	drop	protein	10 (mg/ml)
5	1	drop		10 (mM)
6	1	drop	OGP	1 (%(w/v))
7	1	drop	Tris-HCl	0.2 (mM)