Biological Crystallization
| 1. Verfasser: |
Morales, Jaime Gómez
, [VerfasserIn]
Falini, Giuseppe , [VerfasserIn] García Ruiz, Juan Manuel , [VerfasserIn] |
|---|---|
| Umfang/Format: |
1 online resource (184 pages). |
| Schlagworte: | |
| Online Zugang: |
DOAB: download the publication DOAB: description of the publication |
| LEADER | 04743namaa2201477ui 4500 | ||
|---|---|---|---|
| 001 | 003027806 | ||
| 005 | 20221228154202.0 | ||
| 003 | DE-2553 | ||
| 006 | m o d | ||
| 007 | cr|mn|---annan | ||
| 008 | 20210211s2019 xx |||||o ||| 0|eng d | ||
| 020 | |a books978-3-03921-404-4 | ||
| 020 | |a 9783039214044 | ||
| 020 | |a 9783039214037 | ||
| 040 | |a oapen |c oapen |b eng |d DE-2553 |e rda | ||
| 024 | 7 | |a 10.3390/books978-3-03921-404-4 |c doi | |
| 041 | 0 | |a eng | |
| 042 | |a dc | ||
| 100 | 1 | |a Morales, Jaime Gómez |e author | |
| 264 | |b MDPI - Multidisciplinary Digital Publishing Institute, |c 2019. | ||
| 700 | 1 | |a Falini, Giuseppe |e author | |
| 700 | 1 | |a García Ruiz, Juan Manuel |e author | |
| 245 | 1 | 0 | |a Biological Crystallization |
| 300 | |a 1 online resource (184 pages). | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 506 | 0 | |a Open Access |2 star |f Unrestricted online access | |
| 540 | |a Creative Commons |f https://creativecommons.org/licenses/by-nc-nd/4.0/ |2 cc |4 https://creativecommons.org/licenses/by-nc-nd/4.0/ | ||
| 546 | |a English | ||
| 653 | |a chitosan | ||
| 653 | |a Csep1p | ||
| 653 | |a bond selection during protein crystallization | ||
| 653 | |a bioremediation | ||
| 653 | |a education | ||
| 653 | |a reductants | ||
| 653 | |a heavy metals | ||
| 653 | |a biomimetic crystallization | ||
| 653 | |a MTT assay | ||
| 653 | |a protein crystallization | ||
| 653 | |a drug discovery | ||
| 653 | |a optimization | ||
| 653 | |a polymyxin resistance | ||
| 653 | |a lysozyme | ||
| 653 | |a ependymin-related protein (EPDR) | ||
| 653 | |a equilibration between crystal bond and destructive energies | ||
| 653 | |a barium carbonate | ||
| 653 | |a dyes | ||
| 653 | |a microseed matrix screening | ||
| 653 | |a nanoapatites | ||
| 653 | |a colistin resistance | ||
| 653 | |a Haloalkane dehalogenase | ||
| 653 | |a diffusion | ||
| 653 | |a polyacrylic acid | ||
| 653 | |a random microseeding | ||
| 653 | |a protein 'affinity' to water | ||
| 653 | |a insulin | ||
| 653 | |a protein crystal nucleation | ||
| 653 | |a agarose | ||
| 653 | |a lithium ions | ||
| 653 | |a ependymin (EPN) | ||
| 653 | |a {00.1} calcite | ||
| 653 | |a seeding | ||
| 653 | |a Campylobacter consisus | ||
| 653 | |a metallothioneins | ||
| 653 | |a Crohn's disease | ||
| 653 | |a balance between crystal bond energy and destructive surface energies | ||
| 653 | |a color change | ||
| 653 | |a microbially induced calcite precipitation (MICP) | ||
| 653 | |a crystallization of macromolecules | ||
| 653 | |a crystallization | ||
| 653 | |a calcein | ||
| 653 | |a MCR-1 | ||
| 653 | |a Cry protein crystals | ||
| 653 | |a L-tryptophan | ||
| 653 | |a circular dichroism | ||
| 653 | |a crystal violet | ||
| 653 | |a nanocomposites | ||
| 653 | |a halide-binding site | ||
| 653 | |a calcium carbonate | ||
| 653 | |a PCDA | ||
| 653 | |a ultrasonic irradiation | ||
| 653 | |a adsorption | ||
| 653 | |a biochemical aspects of the protein crystal nucleation | ||
| 653 | |a GTL-16 cells | ||
| 653 | |a proteinase k | ||
| 653 | |a neutron protein crystallography | ||
| 653 | |a classical and two-step crystal nucleation mechanisms | ||
| 653 | |a thermodynamic and energetic approach | ||
| 653 | |a heavy metal contamination | ||
| 653 | |a N-acetyl-D-glucosamine | ||
| 653 | |a crystallization in solution flow | ||
| 653 | |a solubility | ||
| 653 | |a biomorphs | ||
| 653 | |a droplet array | ||
| 653 | |a biomimetic materials | ||
| 653 | |a ferritin | ||
| 653 | |a biomineralization | ||
| 653 | |a wastewater treatment | ||
| 653 | |a H3O+ | ||
| 653 | |a silica | ||
| 653 | |a graphene | ||
| 653 | |a supersaturation dependence of the crystal nucleus size | ||
| 653 | |a pyrrole | ||
| 653 | |a micro-crystals | ||
| 653 | |a nucleation | ||
| 653 | |a crystallography | ||
| 653 | |a mammalian ependymin-related protein (MERP) | ||
| 653 | |a high-throughput | ||
| 653 | |a vaterite transformation | ||
| 653 | |a gradients | ||
| 653 | |a materials science | ||
| 653 | |a bioprecipitation | ||
| 653 | |a biomedicine | ||
| 653 | |a human carbonic anhydrase IX | ||
| 653 | |a protein crystal nucleation in pores | ||
| 653 | |a growth | ||
| 653 | |a crystal growth | ||
| 856 | 4 | 0 | |a www.oapen.org |u https://mdpi.com/books/pdfview/book/1563 |7 0 |z DOAB: download the publication |
| 856 | 4 | 0 | |a www.oapen.org |u https://directory.doabooks.org/handle/20.500.12854/42223 |7 0 |z DOAB: description of the publication |
| 590 | |a Online publication | ||
| 590 | |a ebookoa1222 | ||
| 590 | |a doab | ||
| 942 | |2 z |c EB | ||
| 999 | |c 3027806 |d 1431561 | ||
| 952 | |0 0 |1 0 |2 z |4 0 |6 ONLINE |7 1 |9 973445 |R 2022-12-28 14:42:02 |a DAIG |b DAIG |l 0 |o Online |r 2022-12-28 |y EB | ||
