1URP

D-RIBOSE-BINDING PROTEIN FROM ESCHERICHIA COLI

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	90
Detector technology	IMAGE PLATE
Collection date	1996-06
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	60.099, 120.954, 64.131
Unit cell angles	90.00, 90.05, 90.00

Refinement procedure

Resolution	20.000 - 2.300
Rwork	0.235
R-free	0.26700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	FOR LIGAND-FREE MUTANT RBP MOLECULE B.
RMSD bond length	0.005
RMSD bond angle	1.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.400
High resolution limit [Å]	2.300	2.300
Rmerge	0.056	0.172
Number of reflections	36827
<I/σ(I)>	9.8	4.6
Completeness [%]	90.7	79.1
Redundancy	2	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	5		CRYSTALS WERE OBTAINED FROM SOLUTIONS OF 7.5 - 15 MG/ML RBP, 21% PEG4000, 50-100 MM SODIUM CITRATE, PH 4, 5% GLYCEROL, BY HANGING DROP VAPOUR DIFFUSION., pH 5.0, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7.5-15 (mg/ml)
2	1	reservoir	PEG4000	21 (%)
3	1	reservoir	sodium citrate	50-100 (mM)
4	1	reservoir	glycerol	5 (%)