1BA2

D67R MUTANT OF D-RIBOSE-BINDING PROTEIN FROM ESCHERICHIA COLI

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	90
Detector technology	IMAGE PLATE
Collection date	1996-03
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	47.801, 89.944, 112.276
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.000 - 2.100
R-factor	0.199 *
Rwork	0.199
R-free	0.27900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	SEARCH MODELS REPRESENTING ALL NON-HYDROGEN ATOMS FROM DOMAIN 1 (RESIDUES 1-103 AND 236-264) AND DOMAIN 2 (RESIDUES 104-235 AND 265-271) OF PDB ENTRY 2DRI WERE USED SEPARATELY.
RMSD bond length	0.007 *
RMSD bond angle	1.850 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.000	2.200
High resolution limit [Å]	2.100	2.100
Rmerge	0.038	0.097
Number of reflections	27352
<I/σ(I)>	21.3	7.6
Completeness [%]	94.9	70
Redundancy	3.36	2.04

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7		VAPOR DIFFUSION OF DROPS CONTAINING 7.5 MG/ML PROTEIN AGAINST A RESERVOIR OF 24% PEG4000, 100 MM TRIS-HCL, PH 7., pH 7.0, vapor diffusion

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7.5 (mg/ml)
2	1	reservoir	PEG4000	24 (%)
3	1	reservoir	Tris-HCl	100 (mM)