1N4A

The Ligand Bound Structure of E.coli BtuF, the Periplasmic Binding Protein for Vitamin B12

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Collection date	2002-11-15
Spacegroup name	P 21 21 2
Unit cell lengths	131.730, 92.020, 44.690
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
Rwork	0.234
R-free	0.26200 *
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	22.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.000
Rmerge	0.056 *
Number of reflections	34910
Completeness [%]	98.7 *	91.9 *
Redundancy	4.5 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	294	NaCl, ethanol, acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K
1	VAPOR DIFFUSION, HANGING DROP	4.6	294	NaCl, ethanol, acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mM)
2	1	reservoir		2.0 (M)
3	1	reservoir	ethanol	3 (%)
4	1	reservoir	sodium acetate	100 (mM)	pH4.6