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Updated: Aug 29, 2025

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

A general method for directly phasing diffraction data from high-solvent-content protein crystals.

Richard Lawrence Kingston¹, Rick P Millane²

¹School of Biological Sciences, University of Auckland, 3a Symonds St, Auckland City, Auckland 1010, New Zealand.

|September 8, 2022

Summary

This summary is machine-generated.

This study introduces a novel direct phase determination method for protein crystallography, particularly effective for crystals with high solvent content. The Difference Map algorithm successfully solves phase ambiguity using only diffraction data and solvent estimates.

Keywords:

X-ray crystallography high-solvent-content crystals imaging phasing protein crystals solvent flatness structure determination

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Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

Area of Science:

Structural Biology
Crystallography
Biophysics

Background:

Protein crystallography is crucial for determining protein structures.
Direct phase determination methods are essential for solving the phase problem.
Crystals with high solvent content present unique challenges in phase determination.

Purpose of the Study:

To develop and validate a direct phase determination procedure for protein crystals with high solvent content.
To utilize diffraction data and solvent content estimates as primary inputs.
To treat phase determination as a constraint satisfaction problem.

Main Methods:

Employed the iterative projection Difference Map algorithm.
Broke down the computational process into low-resolution envelope approximation and high-resolution phase determination.
Utilized random phase sets, clustering, and averaging for robust results.

Main Results:

The Difference Map algorithm demonstrated good global convergence properties.
The procedure successfully determined phases without initial phase information.
Robust performance was observed for crystals with solvent fractions > 0.70 at intermediate resolutions (1.9-3.5 Å).

Conclusions:

The developed procedure offers a robust method for direct phase determination in protein crystallography.
High solvent content is a critical factor for the routine success of this method.
The technique is particularly valuable for challenging crystal forms.