1N3Z

Crystal structure of the [S-carboxyamidomethyl-Cys31, S-carboxyamidomethyl-Cys32] monomeric derivative of the bovine seminal ribonuclease in the liganded state

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Wavelength(s)	1.0
Spacegroup name	C 1 2 1
Unit cell lengths	70.690, 28.820, 67.520
Unit cell angles	90.00, 119.20, 90.00

Refinement procedure

Resolution	15.000 - 1.650
R-factor	0.188
Rwork	0.186
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	26.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.680
High resolution limit [Å]	1.650	1.650
Rmerge	0.037	0.098
Total number of observations	99192 *
Number of reflections	14570
<I/σ(I)>	42	14
Completeness [%]	99.9	99.9
Redundancy	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.7	293	PEG 4000, sodium acetate, acetonitrile, glycerol (cryoprotectant), TRIS-HCl, pH 8.7, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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	28 (%(w/v))
3	1	reservoir	Tris-HCl	0.1 (M)	pH8.7
4	1	reservoir	sodium acetate	0.2 (M)
5	1	reservoir	acetonitrile	15 (%(v/v))	pH8.8