1IM0

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT PH 8.3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR591
Temperature [K]	120
Detector technology	IMAGE PLATE
Detector	MAC Science DIP-2000
Wavelength(s)	1.5418
Spacegroup name	P 31 2 1
Unit cell lengths	78.462, 78.462, 101.424
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	21.000 - 2.980
R-factor	0.226 *
Rwork	0.226
R-free	0.26600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1QD5 WITH ACTIVE SITE RESIDUES TRUNCATED TO ALA. ALL WATER AND DETERGENT MOLECULES REMOVED. ALL ATOMS WERE GIVEN A RANDOM SHIFT OF ALMOST 0.5 ANGSTROM.
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]	21.000	3.030
High resolution limit [Å]	2.980	2.980
Rmerge	0.081	0.340
Total number of observations	106289 *
Number of reflections	7686 *	372 *
<I/σ(I)>	24.5	7.9
Completeness [%]	99.6	100
Redundancy	13.7

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)