1KVW

CARBOXYLIC ESTER HYDROLASE, SINGLE MUTANT H48Q OF BOVINE PANCREATIC PLA2 ENZYME

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU R-AXIS II
Temperature [K]	291
Detector technology	IMAGE PLATE
Collection date	1997-01-15
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 31 2 1
Unit cell lengths	47.120, 47.120, 102.880
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 1.950
R-factor	0.209
Rwork	0.209
R-free	0.31400
Structure solution method	THE COORDINATES OF THE WILD TYPE (PDB ENTRY 1MKT) WERE USED AS THE STARTING MODEL FOR REFINEMENT.
Starting model (for MR)	RECOMBINANT PLA2 (1MKT)
RMSD bond length	0.013
RMSD bond angle	23.000 *
Data reduction software	R-AXIS (IIC)
Data scaling software	R-AXIS (II)
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000	2.040
High resolution limit [Å]	1.950	1.950
Rmerge	0.082	0.218
Total number of observations	21567 *
Number of reflections	7424
Completeness [%]	73.0	50
Redundancy	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.2	291 *	CRYSTALS WERE GROWN BY THE VAPOR DIFFUSION METHOD USING THE CONDITIONS 5 (MICRO)L OF THE MUTANT PROTEIN (15MG/ML OF THE PROTEIN), 5MM CACL2, 50MM TRIS BUFFER, PH 7.2 AND 2 (MICRO)L OF 40% MPD AND (60%) OF MPD IN THE RESERVOIR, vapor diffusion

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	11 (mg/ml)
2	1	drop	Tris	7.9 (mM)
3	1	drop		3.6 (mM)
4	1	drop	MPD	14 (%)
5	1	reservoir	MPD	75 (%)