1RHA

WATER DEPENDENT DOMAIN MOTION AND FLEXIBILITY IN RIBONUCLEASE A AND THE INVARIANT FEATURES IN ITS HYDRATION SHELL. AN X-RAY STUDY OF TWO LOW HUMIDITY CRYSTAL FORMS OF THE ENZYME

Experimental procedure

Spacegroup name	P 1 21 1
Unit cell lengths	30.340, 33.270, 52.610
Unit cell angles	90.00, 113.30, 90.00

Refinement procedure

Resolution	10.000 - 1.800
R-factor	0.176
RMSD bond length	0.012
RMSD bond angle	0.040
Refinement software	PROLSQ

Data quality characteristics

	Overall
Low resolution limit [Å]	10.000 *
High resolution limit [Å]	1.800 *
Rmerge	0.027 *
Total number of observations	17852 *
Number of reflections	8667 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Batch method *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	1.5 (%)
2	1	1	ethanol	50 (%)