As suggested by the (conflicting) observations of Eleanor and Nicholas, it’s 
not clear whether you are showing data collection statistics for the full 
resolution range or just for the high resolution shell. If for the whole 
dataset, your Rmerge, I/sigma, and CC1/2 are high, low, and low, respectively; 
if for the high resolution shell, they suggest that you should include higher 
resolution data in your refinement, if available.

See https://doi.org/10.1107/S0907444913000061 and 
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3457925/, and for the standard 
format of reporting these statistics see any crystal structure reported in Acta 
Cryst D.

Best wishes
Kevin

From: CCP4 bulletin board <[email protected]> on behalf of Mandar Bhutkar 
<[email protected]>
Date: Thursday, November 2, 2023 at 12:34 AM
To: [email protected] <[email protected]>
Subject: [ccp4bb] how to increase b factor for water in protein- ligand crystal 
structure
Hi everyone,
I am working on one of the x-ray diffraction data. Refinement details are given 
below. My solvent b factor is 18.44. Can anyone pls suggest me how to improve 
the data?
Thank you.
--
Mr. Mandar Bhutkar,
Ph.D. student,
Molecular Virology lab,
IIT Roorkee.

Resolution range

23.06–2.60

Space group

P 2 21 21

Unit cell dimensions: a b c (Å)

α, β, γ (°)

51.6  60.7 184.36
90      90   90

Completeness (%)

99.3

Rmerge a

0.372

I/σ(I)

2.67

CC(1/2)

0.773

Refinement

Reflections used in refinement

10011

Reflections used for R-free

924

R-workb

0.231

R-freeb

0.273

Wilson B-factor (Å)

28.9

Number of non-hydrogen atoms

4302

Macromolecules

4086

Ligands

94

Solvent

124

Protein residues

508

RMS (bonds) (Å)c

0.01

RMS (angles) (˚) c

1.89

Ramachandran Plot



Favored (%)

97.83

Allowed (%)

1.38

Outliers (%)

0.79

Average B-factor (Å)

28.0

macromolecules (Å)

28.65

ligands (Å)

48.98

solvent (Å)

18.44

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