1OCX

E. coli maltose-O-acetyltransferase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Spacegroup name	C 2 2 21
Unit cell lengths	64.623, 106.238, 175.433
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.150
R-factor	0.198
Rwork	0.194
R-free	0.23500
Structure solution method	OTHER
RMSD bond length	0.016
RMSD bond angle	1.550 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.230
High resolution limit [Å]	2.150	2.150
Rmerge	0.061	0.396
Total number of observations	120930 *
Number of reflections	33084
Completeness [%]	99.7	99.8
Redundancy	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6		HANGING DROP CRYSTALLIZATION CRYSTALS FORM IN A 3 UL (RESERVOIR) + 1 UL (PROTEIN AT 15 MG/ML) DROP WITH RESERVOIR 0.1 M NA CITRATE PH 5.6, 3% ETHANOL, 15 % PEG 4000). ADDITION OF 6 UL OF RESERVOIR AND 1 UL OF 50 MM TRIMETHYL LEAD ACETATE CAUSES CRYSTAL DISSOLUTION AND GROWTH OF CRYSTALS WITH DIFFERENT HABIT FROM WHICH THE STRUCTURE WAS SOLVED.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium citrate	0.1 (M)	pH5.6
2	1	reservoir	ethanol	3 (%)
3	1	reservoir	PEG4000	15 (%)
4	1	drop	protein	15 (mg/ml)