1BDO

STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Detector technology	IMAGE PLATE
Collection date	1993-08-29
Detector	FUJI
Spacegroup name	P 21 21 2
Unit cell lengths	65.460, 37.260, 35.450
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.800
R-factor	0.189
Rwork	0.189
Structure solution method	A MODIFIED MAD PROCEDURE. SOFTWARE USED : NULL STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL
RMSD bond length	0.007
RMSD bond angle	1.540
Data reduction software	DENZO
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	10.000 *
High resolution limit [Å]	1.800 *
Rmerge	0.032
Total number of observations	28655 *
Number of reflections	14891
Completeness [%]	96.4
Redundancy	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *		20 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	sodium citrate	0.96 (M)
3	1	reservoir	borate	7.3 (mM)
4	1	reservoir	DTT	3 (mM)