1MKS

CARBOXYLIC ESTER HYDROLASE, TRIGONAL FORM OF THE TRIPLE MUTANT

Experimental procedure

Temperature [K]	291
Detector technology	IMAGE PLATE
Collection date	1995-12-01
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 31 2 1
Unit cell lengths	47.080, 47.080, 102.370
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 1.900
R-factor	0.186
Rwork	0.186
Structure solution method	THE ATOMIC COORDINATES OF THE NEW HIGH RESOLUTION REFINEMENT OF THE TRIGONAL FORM OF THE NATIVE ENZYME WERE USED AS THE STARTING MODEL (PDB ENTRY 1MKT).
Starting model (for MR)	WILD TYPE
RMSD bond length	0.015
RMSD bond angle	23.100 *
Data reduction software	R-AXIS (IIC)
Data scaling software	R-AXIS (II)
Phasing software	X-PLOR (3.0)
Refinement software	X-PLOR (3.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.000
High resolution limit [Å]	1.820	1.820
Rmerge	0.069	0.194
Total number of observations	12043 *
Number of reflections	7346
<I/σ(I)>		1.72
Completeness [%]	64.0 *	29
Redundancy	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2		CRYSTALS WERE GROWN BY THE HANGING DROP VAPOR DIFFUSION METHOD FROM DROPLETS CONTAINING 5 (MICRO)L OF THE MUTANT PROTEIN (15MG/ML) 5MM CACL2, 50MM TRIS BUFFER, PH 7.2 AND 2 (MICRO)L OF 75% MPD AND (50%) OF MPD IN THE RESERVOIR, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10.7 (mg/ml)
2	1	drop		3.6 (mM)
3	1	drop	Tris-HCl	35.7 (mM)
4	1	drop	MPD	21.4 (%)
5	1	reservoir	MPD	50 (%)