1ATG

AZOTOBACTER VINELANDII PERIPLASMIC MOLYBDATE-BINDING PROTEIN

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-09
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	32.934, 88.802, 41.746
Unit cell angles	90.00, 93.55, 90.00

Refinement procedure

Resolution	40.000 - 1.200
R-factor	0.164 *
Rwork	0.164
R-free	0.18354 *
Structure solution method	SINGLE ISOMORPHOUS REPLACEMENT WITH ANOMALOUS SCATTERING
RMSD bond length	0.007
RMSD bond angle	0.020
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4 ((MLPHARE)
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	1.220
High resolution limit [Å]	1.200	1.200
Rmerge	0.094	0.161
Number of reflections	74061
<I/σ(I)>	12.7	6.9
Completeness [%]	99.4	99.1
Redundancy	3.7	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	18 *	HANGING DROP VAPOUR DIFFUSION WITH PROTEIN CONCENTRATION IN THE RANGE 10-15 MG/ML IN 10MM TRIS-HCL PH 7.0. 1 OR 2 MICROLITER DROPS OF THE LATTER WERE MIXED WITH AN EQUAL VOLUME OF 11-14% (W/V) PEG 4000 AND 0.4M AMMONIUM SULFATE IN 0.1M ACETATE BUFFER AT PH 4.0, AND THEN EQUILIBRATED AGAINST THIS SOLUTION AT 18 DEG C. CRYOPROTECTED USING THE SAME SOLUTION CONTAINING 25% (V/V) ETHYLENE GLYCOL., vapor diffusion - hanging drop, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-15 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)
3	1	drop	sodium molybdate	1 (mM)	can be replaced by 1mM sodium tungstate
4	1	reservoir	PEG4000	11-14 (%(w/v))
5	1	reservoir	ammonium sulfate	0.4 (M)
6	1	reservoir	sodium acetate	0.1 (M)