1KH8

Structure of a cis-proline (P114) to glycine variant of Ribonuclease A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	288
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS II
Wavelength(s)	1.5418
Spacegroup name	P 43 21 2
Unit cell lengths	40.870, 40.870, 129.250
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.000
Rwork	0.195
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	High Salt Wild Type RNase A (PAUL: Kim et al Biochemistry 1992 31 12304-12314)
RMSD bond length	0.005
RMSD bond angle	1.200
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.053 *
Number of reflections	7592 *
Completeness [%]	94.7	82.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	6.6	303	NaPO4, CsCl2, ammonium sulfate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 303K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	5 (mg/ml)
2	1	1		0.15 (M)
3	1	1		3 (M)	pH6.6
4	1	2	ammonium sulfate	30 (%sat)