5BIR

DISECTING HISTIDINE INTERACTIONS IN RIBONUCLEASE T1 USING ASN AND GLN MUTATIONS

Experimental procedure

Source details	ENRAF-NONIUS
Temperature [K]	293
Detector technology	DIFFRACTOMETER
Collection date	1996-02-20
Detector	ENRAF-NONIUS FAST
Spacegroup name	P 41 21 2
Unit cell lengths	58.390, 58.390, 133.390
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.850 *
R-factor	0.193
Rwork	0.193
R-free	0.25600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2aad
RMSD bond length	0.031
RMSD bond angle	26.800 *
Data reduction software	ROTAVATA
Data scaling software	CCP4 ((AGROVATA)
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000	1.950
High resolution limit [Å]	1.850 *	1.850
Rmerge	0.050 *	0.038 *
Total number of observations	94960 *
Number of reflections	19597 *
<I/σ(I)>	10.1	7.2
Completeness [%]	96.0	90.7
Redundancy	1.3	1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.2		VAPOR DIFFUSION, HANGING DROP, 20 MG/ML PROTEIN NAOAC BUF. PH 4.2, 0.125 % 2'GMP, 1.25 % CACL2, 47.5 % MPD, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir		50 (mM)
3	1	reservoir	MPD	47.5 (%)
4	1	reservoir	2'-GMP	0.125 (%)
5	1	reservoir		1.25 (%)