Refinement of Macromolecular Structures by the Maximum‐Likelihood Method

Refinement of Macromolecular Structures by the Maximum‐Likelihood Method This paper reviews the mathematical basis of maximum likelihood. The likelihood function for macromolecular structures is extended to include prior phase information and experimental standard uncertainties. The assumption that different parts of a structure might have different errors is considered. A method for estimating σA using `free' reflections is described and its effects analysed. The derived equations have been implemented in the program REFMAC. This has been tested on several proteins at different stages of refinement (bacterial α‐amylase, cytochrome c′, cross‐linked insulin and oligopeptide binding protein). The results derived using the maximum‐likelihood residual are consistently better than those obtained from least‐squares refinement. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section D Wiley

Refinement of Macromolecular Structures by the Maximum‐Likelihood Method

Loading next page...
 
/lp/wiley/refinement-of-macromolecular-structures-by-the-maximum-likelihood-pBzuzT2OUS
Publisher
Wiley
Copyright
Copyright © 1997 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1399-0047
eISSN
1399-0047
D.O.I.
10.1107/S0907444996012255
Publisher site
See Article on Publisher Site

Abstract

This paper reviews the mathematical basis of maximum likelihood. The likelihood function for macromolecular structures is extended to include prior phase information and experimental standard uncertainties. The assumption that different parts of a structure might have different errors is considered. A method for estimating σA using `free' reflections is described and its effects analysed. The derived equations have been implemented in the program REFMAC. This has been tested on several proteins at different stages of refinement (bacterial α‐amylase, cytochrome c′, cross‐linked insulin and oligopeptide binding protein). The results derived using the maximum‐likelihood residual are consistently better than those obtained from least‐squares refinement.

Journal

Acta Crystallographica Section DWiley

Published: May 1, 1997

There are no references for this article.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off