Next Article in Journal / Special Issue
Radiation Damage in Macromolecular Crystallography—An Experimentalist’s View
Previous Article in Journal
Cobalt(II) Terpyridin-4′-yl Nitroxide Complex as an Exchange-Coupled Spin-Crossover Material
Previous Article in Special Issue
Conformational Flexibility of Proteins Involved in Ribosome Biogenesis: Investigations via Small Angle X-ray Scattering (SAXS)
Article Menu
Issue 4 (April) cover image

Export Article

Open AccessArticle

Resolution Dependence of an Ab Initio Phasing Method in Protein X-ray Crystallography

Department of Physics and Texas Center for Superconductivity, University of Houston, Houston, TX 77204, USA
*
Author to whom correspondence should be addressed.
Crystals 2018, 8(4), 156; https://doi.org/10.3390/cryst8040156
Received: 17 February 2018 / Revised: 30 March 2018 / Accepted: 31 March 2018 / Published: 3 April 2018
(This article belongs to the Special Issue Recent Advances in Protein Crystallography)
  |  
PDF [8342 KB, uploaded 3 May 2018]
  |  

Abstract

For direct phasing of protein crystals, a method based on the hybrid-input-output (HIO) algorithm has been proposed and tested on a variety of structures. So far, however, the diffraction data have been limited to high-resolution ones, i.e., higher than 2 Å. In principle, the methodology can be applied to data of lower resolutions, which might be particularly useful for phasing membrane protein crystals. For resolutions higher than 3.5 Å, it seems the atomic structure is solvable. For data of lower resolutions, information of the secondary structures and the protein boundary can still be obtained. Examples are given to support the conclusions. Real experimental data are used. Two aspects of the observed data have been discussed: removal of the measured low-resolution reflections and involvement of the unmeasured high-resolution reflections. The ab initio phasing employs histogram matching for density modification. A question arises whether the reference histogram used should match the resolution of the diffraction data or not. It seems that there is an optimal histogram which is good to use for data at various resolutions. View Full-Text
Keywords: resolution dependence; hybrid input-output; iterative projection algorithm; ab initio phasing; membrane protein; X-ray crystallography resolution dependence; hybrid input-output; iterative projection algorithm; ab initio phasing; membrane protein; X-ray crystallography
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Jiang, M.; He, H.; Cheng, Y.; Su, W.-P. Resolution Dependence of an Ab Initio Phasing Method in Protein X-ray Crystallography. Crystals 2018, 8, 156.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Crystals EISSN 2073-4352 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top