1B0D

Structural effects of monovalent anions on polymorphic lysozyme crystals

Experimental procedure

Experimental method	MONOCHROMATIC
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1994-04-01
Detector	RIGAKU RAXIS II
Spacegroup name	P 43 21 2
Unit cell lengths	79.060, 79.060, 37.970
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.000 - 1.840
Rwork	0.202
R-free	0.24100
Structure solution method	OTHER
RMSD bond length	0.008 *
RMSD bond angle	1.320 *
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	CCP4
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	13.500	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.049 *	0.135 *
Number of reflections	10484 *
<I/σ(I)>	10.5	4.5
Completeness [%]	97.5	85.8
Redundancy	6.6	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.5	291	drop consists of equal volume of protein and reservoir solutions *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	deionized lysozyme	40.4 (mg/ml)
2	1	drop		50 (mM)
3	1	reservoir	NapTS	90 (mM)
4	1	reservoir		50 (mM)