Identifying, studying and making good use of macromolecular crystals

被引：18

作者：

Calero, Guillermo ^{[1
]}

Cohen, Aina E. ^{[2
]}

Luft, Joseph R. ^{[3
,4
]}

Newman, Janet ^{[5
]}

Snell, Edward H. ^{[3
,4
]}

机构：

[1] Univ Pittsburgh, Sch Med, Dept Struct Biol, Pittsburgh, PA 15261 USA

[2] Stanford Univ, SLAC Natl Accelerator Lab, Stanford Synchrotron Radiat Lightsource, Menlo Pk, CA 94025 USA

[3] Hauptman Woodward Med Res Inst, Buffalo, NY 14203 USA

[4] SUNY Buffalo, Dept Struct Biol, Buffalo, NY 14203 USA

[5] CSIRO Collaborat Crystallisat Ctr, Parkville, Vic 3052, Australia

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

基金：

美国国家卫生研究院;

关键词：

MEMBRANE-PROTEIN CRYSTALS; CRYSTALLIZATION CONDITIONS; LIGHT-SCATTERING; VISUAL ANALYSIS; CONTROL-SYSTEM; TRAINING SET; DIFFRACTION; FLUORESCENCE; CRYSTALLOGRAPHY; RADIATION;

D O I：

10.1107/S2053230X14016574

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Structural biology has contributed tremendous knowledge to the understanding of life on the molecular scale. The Protein Data Bank, a depository of this structural knowledge, currently contains over 100 000 protein structures, with the majority stemming from X-ray crystallography. As the name might suggest, crystallography requires crystals. As detectors become more sensitive and X-ray sources more intense, the notion of a crystal is gradually changing from one large enough to embellish expensive jewellery to objects that have external dimensions of the order of the wavelength of visible light. Identifying these crystals is a prerequisite to their study. This paper discusses developments in identifying these crystals during crystallization screening and distinguishing them from other potential outcomes. The practical aspects of ensuring that once a crystal is identified it can then be positioned in the X-ray beam for data collection are also addressed.

引用

页码：993 / 1008

页数：16

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