8F28

Lysozyme Structures from Single-Entity Crystallization Method NanoAC

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.1
Synchrotron site	ALS
Beamline	8.2.1
Temperature [K]	100
Detector technology	CCD
Collection date	2020-11-06
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.0000
Spacegroup name	P 43 21 2
Unit cell lengths	78.592, 78.592, 36.815
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.690 - 1.200
R-factor	0.144
Rwork	0.142
R-free	0.17030
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1iee
RMSD bond length	0.006
RMSD bond angle	0.855
Data scaling software	HKL-2000
Phasing software	PHENIX (1.20)
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.220
High resolution limit [Å]	1.200	3.260	1.200
Rmerge	0.073	0.055	0.268
Rmeas	0.079	0.060	0.346
Rpim	0.028	0.022	0.215
Total number of observations	246464
Number of reflections	35301	1975	1298
<I/σ(I)>	20.1
Completeness [%]	96.4	97.3	71.2
Redundancy	7	7.8	2
CC(1/2)		0.993	0.852

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	LIQUID DIFFUSION	4.8	295	A new crystallization method named NanoAC was used. Protein solution and precipitant solution were connected through a single nanopipette to control (in time and space) nucleation and crystal growth