Dear John,
In protein crystallography, the ranges customarily applied to
resolution are:
Low resolution --> worse than 2.7 A
Medium resolution --> better than 2.7 A but worse than 1.8 A
High resolution --> better than 1.8 A and worse than 1.2 A
Atomic resolution --> better than 1.2 A and worse than 0.95 A
Ultra high resolution --> better than 0.95 A
There is a very nice diagram for you in Fig. 5 of Wlodawer et al., FEBS J.
2008 Jan; 275(1): 1–21.
<https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&retmode=ref&cmd=prlinks&id=18034855>:
at this link:
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4465431/figure/F5/
You should think in terms of reciprocal space and diffraction.
Higher angle of diffraction w.r.t. the incident beam means High Resolution,
which means lower number.
Best wishes,
Natesh
On 5 February 2017 at 17:39, <John Pontty> <
[email protected]> wrote:
> Dear All,
>
> For one protein crystal, its resolution was 1.8 A. For another crystal for
> the same protein, its resolution was 3.8 A. In literature, do we call the
> 1.8 A crystal as the high resolution crystal (because of quality), or do we
> call the 3.8 A crystal as the high resolution crystal (because of 3.8 was
> larger than 1,8)?
>
> Best regards.
>
> John
>
--
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"Live Simply and do Serious Things .. "
- Dorothy Mary Crowfoot Hodgkin OM, FRS
"In Science truth always wins"
- Max Ferdinand Perutz OM FRS
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Dr. Ramanathan Natesh
Ramalingaswami Fellow-DBT, Assistant Professor
Indian Institute of Science Education and Research Thiruvananthapuram
(IISER-TVM),
1st floor, Dept. of Computer Science & Engg. Building,
CET Campus, Engineering College P.O.,
Trivandrum, 695016, Kerala, India
[email protected]
http://www.researcherid.com/rid/C-4488-2008
http://faculty.iisertvm.ac.in/~natesh
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