1UCA

Crystal structure of the Ribonuclease MC1 from bitter gourd seeds complexed with 2'-UMP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	298
Detector technology	CCD
Collection date	1999-10-12
Detector	MARRESEARCH
Wavelength(s)	0.7
Spacegroup name	P 21 21 21
Unit cell lengths	38.810, 67.940, 75.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.480
Rwork	0.194
R-free	0.21300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bk7
RMSD bond length	0.005
RMSD bond angle	1.658 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.400	1.560
High resolution limit [Å]	1.480	1.480
Rmerge	0.075	0.500
Total number of observations	335854 *
Number of reflections	31397
<I/σ(I)>	6.8	1.5
Completeness [%]	92.9	91.7
Redundancy	3.6	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.7	293	PEG 8000, sodium acetate, sodium cacodylate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	19 (mg/ml)
2	1	reservoir	sodium acetate	0.2 (M)
3	1	reservoir	sodium cacodylate	0.1 (M)	pH6.7
4	1	reservoir	PEG8000	21 (%)
5	1	reservoir	2'-UMP	10 (mM)