1ILD

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR591
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1999-01-15
Detector	MAC Science DIP-2000
Spacegroup name	P 31 2 1
Unit cell lengths	78.484, 78.484, 101.669
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.800
R-factor	0.211 *
Rwork	0.211
R-free	0.27500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1QD5 MUTATED ACTIVE SITE RESIDUES to ALA AND GAVE ALL ATOMS A RANDOM SHIFT
RMSD bond length	0.007
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.850
High resolution limit [Å]	2.800	2.800
Rmerge	0.064	0.343
Total number of observations	98747 *
Number of reflections	9276	453 *
<I/σ(I)>	25.4	4.9
Completeness [%]	99.3	99.6
Redundancy	10

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.6 *	293	MPD, calcium chloride, Bis-Tris buffer, pH 6.0, 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)