1UBC

Structure of Reca Protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	2000-11-05
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 61
Unit cell lengths	103.441, 103.441, 71.765
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 * - 3.800
R-factor	0.242
Rwork	0.242
R-free	0.30500 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1g19
RMSD bond length	0.010 *
RMSD bond angle	1.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.940
High resolution limit [Å]	3.800	3.800
Rmerge	0.152 *	0.479 *
Number of reflections	4340	434 *
<I/σ(I)>		2
Completeness [%]	98.5	99.3
Redundancy	4.6	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	PEG 4000, CIT-PHOS, NACL, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	drop	citrate-phosphate	100 (mM)	pH7.5
3	1	drop		100 (mM)
4	1	drop	dithiothreitol	0.2 (mM)
5	1	drop	ammonium acetate	0.1 (M)
6	1	drop	PEG4000	6 (%)
7	1	reservoir	PEG4000	25 (%)